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Searching for up to 100 curated homologs for Ac3H11_631 FitnessBrowser__acidovorax_3H11:Ac3H11_631 (351 a.a.)

Found high-coverage hits (≥70%) to 25 curated proteins.

You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.

Hits with ≥ 30% identity

METN_BACSU / O32169 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Bacillus subtilis (strain 168) (see paper)
TC 3.A.1.24.2 / O32169 MetN (C) (aka YusC), component of The L- and D-methionine porter (also transports methionine sulfoxide from Bacillus subtilis subsp. subtilis str. 168 (see 2 papers)
    47% identity, 99% coverage of query (338 bits)

MetN / b0199 L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) from Escherichia coli K-12 substr. MG1655 (see 4 papers)
MetN / P30750 L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) from Escherichia coli (strain K12) (see 3 papers)
METN_ECOLI / P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 7 papers)
P30750 ABC-type methionine transporter (subunit 2/2) (EC 7.4.2.11) from Escherichia coli (see 3 papers)
TC 3.A.1.24.1 / P30750 MetN, D-methionine transport ATP-binding protein, component of The L- and D-methionine porter (also transports formyl-L-methionine and other methionine derivatives) (Zhang et al., 2003). The 3.7A structure of MetNI has been solved. An allosteric regulatory mechanism operates at the level of transport activity, so increased intracellular levels of the transported ligand stabilize an inward-facing, ATPase-inactive state of MetNI to inhibit further ligand translocation into the cell from Escherichia coli (see 5 papers)
    47% identity, 98% coverage of query (309 bits)

6cvlD / P30750 Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
    46% identity, 98% coverage of query (308 bits)

3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form
    46% identity, 98% coverage of query (308 bits)

3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form
    46% identity, 98% coverage of query (308 bits)

TC 3.A.1.24.5 / Q9HT70 Methionine import ATP-binding protein MetN 2, component of L-Histidine uptake porter, MetIQN from Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    47% identity, 98% coverage of query (299 bits)

TC 3.A.1.24.3 / Q8K8K8 AtmD (MetN), component of The methionine porter, AtmBDE from Streptococcus pyogenes serotype M3 (see 2 papers)
    44% identity, 98% coverage of query (287 bits)

TC 3.A.1.24.4 / Q8NSN2 Methionine import ATP-binding protein metN, component of L-Methionine uptake porter, MetQNI from Corynebacterium glutamicum (see paper)
    45% identity, 92% coverage of query (278 bits)

TcyN / b1917 cystine ABC transporter ATP binding subunit (EC 7.4.2.12) from Escherichia coli K-12 substr. MG1655 (see 8 papers)
tcyN / P37774 cystine ABC transporter ATP binding subunit (EC 7.4.2.12) from Escherichia coli (strain K12) (see 7 papers)
TCYN_ECOLI / P37774 L-cystine transport system ATP-binding protein TcyN; EC 7.4.2.12 from Escherichia coli (strain K12) (see 5 papers)
TC 3.A.1.3.10 / P37774 YECC aka CysZ aka B1917, component of Cystine/cysteine/diaminopimelate transporter, CysXYZ; these proteins are also designated FliY/YecS/YecC from Escherichia coli (see 5 papers)
    42% identity, 70% coverage of query (184 bits)

MALK_SALTY / P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
    35% identity, 72% coverage of query (142 bits)

MalK / b4035 maltose ABC transporter ATP binding subunit (EC 7.5.2.1) from Escherichia coli K-12 substr. MG1655 (see 31 papers)
MalK / P68187 maltose ABC transporter ATP binding subunit (EC 7.5.2.1) from Escherichia coli (strain K12) (see 29 papers)
MALK_ECOLI / P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 6 papers)
P68187 ABC-type maltose transporter (subunit 3/3) (EC 7.5.2.1) from Escherichia coli (see paper)
TC 3.A.1.1.1 / P68187 Maltose/maltodextrin import ATP-binding protein MalK aka B4035, component of Maltooligosaccharide porter. The 3-D structure has been reported by Oldham et al. (2007). An altering access mechanism has been suggested for the maltose transporter resulting from rigid-body rotations (Khare et al., 2009). Bordignon et al. (2010) and Schneider et al. (2012) have reviewed the extensive knowledge available on MalEFGK2, its mode of action and its regulatory interactions from Escherichia coli (see 17 papers)
malK / RF|NP_418459 maltose/maltodextrin import ATP-binding protein malK; EC 3.6.3.19 from Escherichia coli K12 (see 18 papers)
    35% identity, 72% coverage of query (141 bits)

2awnB / P68187 Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
    35% identity, 72% coverage of query (141 bits)

1q12A Crystal structure of the atp-bound e. Coli malk
    35% identity, 72% coverage of query (141 bits)

3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state
    35% identity, 72% coverage of query (141 bits)

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3
    35% identity, 72% coverage of query (141 bits)

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4
    35% identity, 72% coverage of query (141 bits)

3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4
    35% identity, 72% coverage of query (141 bits)

ECFA1_STRT2 / Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA1; ECF transporter A component EcfA1; EC 7.-.-.- from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) (see paper)
TC 3.A.1.25.6 / Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA 2, component of Riboflavin ECF transport system, EcfAA'T/RibU from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
    35% identity, 72% coverage of query (136 bits)

8hplC / A0R2C0 Lpqy-sugabc in state 1 (see paper)
    31% identity, 71% coverage of query (120 bits)

7z15I / P16678 E. Coli c-p lyase bound to a phnk/phnl dual abc dimer and adp + pi (see paper)
    32% identity, 71% coverage of query (115 bits)

7niwA / P21439 Nanodisc reconstituted human abcb4 in complex with 4b1-fab (posaconazole-bound, inward-open conformation) (see paper)
    33% identity, 80% coverage of query (115 bits)

6s7pA Nucleotide bound abcb4
    33% identity, 80% coverage of query (112 bits)

Build an alignment

Build an alignment for Ac3H11_631 and 22 homologs with ≥ 30% identity

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Additional hits (identity < 30%)

7lkpA Structure of atp-free human abca4
    25% identity, 72% coverage of query (86.7 bits)

ABCA4_HUMAN / P78363 Retinal-specific phospholipid-transporting ATPase ABCA4; ATP-binding cassette sub-family A member 4; RIM ABC transporter; RIM proteinv; RmP; Retinal-specific ATP-binding cassette transporter; Stargardt disease protein; EC 7.6.2.1 from Homo sapiens (Human) (see 38 papers)
TC 3.A.1.211.2 / P78363 The retinal-specific ABC transporter (RIM protein, ABCR or ABCA4) (Stargardt's disease protein, involved in retinal/macular degeneration) in the rod outer segment. Changes in the oligomeric state of the nucleotide binding domains of ABCR are coupled to ATP hydrolysis and might represent a signal for the TMDs of ABCR to export the bound substrate (Biswas-Fiss 2006). The ABCA4 porter flips N-retinylidene-phosphatidylethanolamine, a product generated from the photobleaching of rhodopsin, from the lumen to the cytoplasmic side of disc membranes following the photobleaching of rhodopsin, insuring that retinoids do not accumulate in disc membranes (Molday, 2007; Molday et al. 2009; Tsybovsky et al. 2013). It also transports several vitamin A derivatives (Sun, 2011) and phosphatidylethanolamine in the same direction. Mutations, known to cause Stargardt disease, decrease N-retinylidene-phosphatidylethanolamine and phosphatidylethanolamine transport activities (Quazi et al. 2012). It functions as an inwardly directed retinoid flippase in the visual cycle from Homo sapiens (Human) (see 28 papers)
    26% identity, 72% coverage of query (85.9 bits)

7lkzA Structure of atp-bound human abca4
    25% identity, 72% coverage of query (84.3 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory