Family Search for PF06155 (GBBH-like

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Family Search for PF06155 (GBBH-like_N)

April 2024: See Interactive Tools for Functional Annotation of Bacterial Genomes for advice on using these tools.

Running HMMer for PF06155

PF06155 hits 44 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

Sama_0429 predicted FeS cluster maintenance protein from Shewanella amazonensis SB2B
Aligns to 9:91 / 126 (65.9%), covers 98.8% of PF06155, 107.8 bits

mutant phenotype: PFam PF06155.8 (DUF971). conserved cofitness with mrp/apbC (Sama_2048)

SO4164 predicted FeS cluster maintenance protein from Shewanella oneidensis MR-1
Aligns to 11:93 / 128 (64.8%), covers 98.8% of PF06155, 105.9 bits

mutant phenotype: PFam PF06155.8 (DUF971). conserved cofitness with mrp/apbC (SO2618) and perhaps bolA

Pf1N1B4_1554 predicted FeS cluster maintenance protein from Pseudomonas fluorescens FW300-N1B4
Aligns to 8:90 / 125 (66.4%), covers 100.0% of PF06155, 94.7 bits

mutant phenotype: PFam PF06155.8 (DUF971). Conserved cofitness with mrp/apbC (Pf1N1B4_731)

AO353_12420 predicted FeS cluster maintenance protein from Pseudomonas fluorescens FW300-N2E3
Aligns to 9:91 / 126 (65.9%), covers 100.0% of PF06155, 91.9 bits

mutant phenotype: PFam PF06155.8 (DUF971). conserved cofitness with yggX (AO353_12045), nfuA (AO353_21625)

P80193 γ-butyrobetaine hydroxylase subunit (EC 1.14.11.1) from Pseudomonas sp. (strain AK-1) (see 5 papers)
P80193 gamma-butyrobetaine dioxygenase (EC 1.14.11.1) from Pseudomonas sp. (see 2 papers)
Aligns to 19:101 / 383 (21.7%), covers 89.4% of PF06155, 62.0 bits

Bbox1 / Q9QZU7 γ-butyrobetaine hydroxylase subunit (EC 1.14.11.1) from Rattus norvegicus (see paper)
BODG_RAT / Q9QZU7 Gamma-butyrobetaine dioxygenase; Gamma-butyrobetaine hydroxylase; Gamma-BBH; Gamma-butyrobetaine,2-oxoglutarate dioxygenase; EC 1.14.11.1 from Rattus norvegicus (Rat) (see paper)
Q9QZU7 gamma-butyrobetaine dioxygenase (EC 1.14.11.1) from Rattus norvegicus (see paper)
Aligns to 9:92 / 387 (21.7%), covers 91.8% of PF06155, 61.7 bits

function: Catalyzes the formation of L-carnitine from gamma- butyrobetaine
catalytic activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate (RHEA:24028)
cofactor: Fe(2+) (Binds 1 Fe(2+) ion per subunit.)
cofactor: L-ascorbate

BBOX1 / O75936 γ-butyrobetaine dioxygenase (EC 1.14.11.1) from Homo sapiens (see 4 papers)
BODG_HUMAN / O75936 Gamma-butyrobetaine dioxygenase; Gamma-butyrobetaine hydroxylase; Gamma-BBH; Gamma-butyrobetaine,2-oxoglutarate dioxygenase; EC 1.14.11.1 from Homo sapiens (Human) (see paper)
O75936 gamma-butyrobetaine dioxygenase (EC 1.14.11.1) from Homo sapiens (see 5 papers)
Aligns to 9:92 / 387 (21.7%), covers 90.6% of PF06155, 59.2 bits

function: Catalyzes the formation of L-carnitine from gamma- butyrobetaine
catalytic activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate (RHEA:24028)
cofactor: Fe(2+) (Binds 1 Fe(2+) ion per subunit.)
cofactor: L-ascorbate

STR8_STRTC / A0A384XR80 Dioxygenase str8; Strobilurin A biosynthesis cluster protein r8; EC 1.14.-.- from Strobilurus tenacellus (see 3 papers)
Aligns to 58:129 / 422 (17.1%), covers 76.5% of PF06155, 52.7 bits

function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain (PubMed:30258052). Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia- lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 (PubMed:30258052). Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A (PubMed:30258052). The FAD- dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore (PubMed:30258052). Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable). Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the production of strobilurin A (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol (PubMed:30258052). The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable). It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable). Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable). Finally, no obvious self- resistance gene is found within the cluster (Probable).
cofactor: Fe(2+) (Binds 1 Fe(2+) ion per subunit.)

TMLH_MOUSE / Q91ZE0 Trimethyllysine dioxygenase, mitochondrial; Epsilon-trimethyllysine 2-oxoglutarate dioxygenase; TML hydroxylase; TML-alpha-ketoglutarate dioxygenase; TML dioxygenase; TMLD; EC 1.14.11.8 from Mus musculus (Mouse) (see paper)
Q91ZE0 trimethyllysine dioxygenase (EC 1.14.11.8) from Mus musculus (see 2 papers)
Aligns to 51:134 / 421 (20.0%), covers 96.5% of PF06155, 47.6 bits

function: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
catalytic activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 = (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate (RHEA:14181)
cofactor: Fe(2+) (Binds 1 Fe(2+) ion per subunit.)
cofactor: L-ascorbate
subunit: Homodimer.

Tmlhe / Q91ZW6 ε-N-trimethyllysine hydroxylase subunit (EC 1.14.11.8) from Rattus norvegicus (see paper)
TMLH_RAT / Q91ZW6 Trimethyllysine dioxygenase, mitochondrial; Epsilon-trimethyllysine 2-oxoglutarate dioxygenase; TML hydroxylase; TML-alpha-ketoglutarate dioxygenase; TML dioxygenase; TMLD; EC 1.14.11.8 from Rattus norvegicus (Rat) (see paper)
Q91ZW6 trimethyllysine dioxygenase (EC 1.14.11.8) from Rattus norvegicus (see paper)
Aligns to 51:134 / 421 (20.0%), covers 96.5% of PF06155, 47.2 bits

function: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML) (PubMed:11431483).
catalytic activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 = (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate (RHEA:14181)
cofactor: Fe(2+) (Binds 1 Fe(2+) ion per subunit.)
cofactor: L-ascorbate
subunit: Homodimer.

TMLHE / Q9NVH6 trimethyllysine dioxygenase, mitochondrial (EC 1.14.11.8) from Homo sapiens (see 4 papers)
TMLH_HUMAN / Q9NVH6 Trimethyllysine dioxygenase, mitochondrial; Epsilon-trimethyllysine 2-oxoglutarate dioxygenase; Epsilon-trimethyllysine hydroxylase; TML hydroxylase; TML-alpha-ketoglutarate dioxygenase; TML dioxygenase; TMLD; EC 1.14.11.8 from Homo sapiens (Human) (see 7 papers)
Q9NVH6 trimethyllysine dioxygenase (EC 1.14.11.8) from Homo sapiens (see 6 papers)
Aligns to 37:134 / 421 (23.3%), covers 95.3% of PF06155, 45.2 bits

function: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML) (PubMed:11431483, PubMed:23092983).
catalytic activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 = (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate (RHEA:14181)
cofactor: Fe(2+) (Binds 1 Fe(2+) ion per subunit.)
cofactor: L-ascorbate
subunit: Homodimer.

tmpA / A0A4V8H042 (2-trimethylamino)ethylphosphonate dioxygenase (EC 1.14.11.72) from Leisingera caerulea (see paper)
TMPA_LEICA / A0A4V8H042 [2-(trimethylamino)ethyl]phosphonate dioxygenase; TMAEP hydroxylase; EC 1.14.11.72 from Leisingera caerulea (Phaeobacter caeruleus) (see paper)
A0A4V8H042 [2-(trimethylamino)ethyl]phosphonate dioxygenase (EC 1.14.11.72) from Leisingera caerulea (see paper)
Aligns to 5:90 / 377 (22.8%), covers 94.1% of PF06155, 33.8 bits

function: Involved in the degradation of the naturally occurring organophosphonate 2-(trimethylammonio)ethylphosphonate (TMAEP) (PubMed:30789718). Catalyzes the hydroxylation of TMAEP to (R)-1- hydroxy-2-(trimethylammonio)ethylphosphonate (OH-TMAEP) (PubMed:30789718). Is highly specific for its N-trimethylated substrate (PubMed:30789718). Cannot use gamma-butyrobetaine as substrate (PubMed:30789718).
catalytic activity: 2-oxoglutarate + [2-(trimethylamino)ethyl]phosphonate + O2 = [(1R)-1-hydroxy-2-(trimethylamino)ethyl]phosphonate + CO2 + succinate (RHEA:11380)
cofactor: Fe(2+) (Binds 1 Fe(2+) ion per subunit.)
cofactor: L-ascorbate
subunit: Homodimer.

HF101_ARATH / Q6STH5 Fe-S cluster assembly factor HCF101, chloroplastic; Protein HIGH CHLOROPHYLL FLUORESCENCE 101 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
Aligns to 431:516 / 532 (16.2%), covers 69.4% of PF06155, 31.7 bits

function: Required for photosystem I (PSI) biosynthesis and assembly. May serve as a chloroplast scaffold protein that specifically assembles iron-sulfur (4Fe-4S) clusters and transfers them to the chloroplast PSI and ferredoxin-thioredoxin (FTR) complexes. Can assemble a 4Fe-4S cluster and transfer it to apoproteins in yeast cells. Probably not required for assembly or stability of plastidic 2Fe-2S clusters.
cofactor: [4Fe-4S] cluster (Binds 1 [4Fe-4S] cluster.)
disruption phenotype: Seedling lethality when homozygous due to impaired photosystem I (PSI).

Or search for genetic data about PF06155 in the Fitness Browser

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory