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Database: UniProt
Entry: A0A0C1GYB4_9RHOB
LinkDB: A0A0C1GYB4_9RHOB
Original site: A0A0C1GYB4_9RHOB 
ID   A0A0C1GYB4_9RHOB        Unreviewed;       402 AA.
AC   A0A0C1GYB4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KIC44173.1};
GN   ORFNames=RA28_14480 {ECO:0000313|EMBL:KIC44173.1};
OS   Ruegeria sp. ANG-S4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC44173.1, ECO:0000313|Proteomes:UP000031326};
RN   [1] {ECO:0000313|Proteomes:UP000031326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the formate dehydrogenase gamma subunit family.
CC       {ECO:0000256|ARBA:ARBA00010747}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIC44173.1}.
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DR   EMBL; JWLK01000005; KIC44173.1; -; Genomic_DNA.
DR   RefSeq; WP_039530243.1; NZ_JWLK01000005.1.
DR   AlphaFoldDB; A0A0C1GYB4; -.
DR   STRING; 1577904.RA28_14480; -.
DR   OrthoDB; 9790598at2; -.
DR   Proteomes; UP000031326; Unassembled WGS sequence.
DR   GO; GO:0009326; C:formate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   Gene3D; 1.20.950.20; Transmembrane di-heme cytochromes, Chain C; 1.
DR   InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   InterPro; IPR006471; Formate_DH_gsu.
DR   NCBIfam; TIGR01583; formate-DH-gamm; 1.
DR   PANTHER; PTHR30074:SF6; BLL5475 PROTEIN; 1.
DR   PANTHER; PTHR30074; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, CYTOCHROME B556 FDN SUBUNIT; 1.
DR   Pfam; PF01292; Ni_hydr_CYTB; 1.
DR   SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031326};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..402
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002150858"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          164..369
FT                   /note="Cytochrome b561 bacterial/Ni-hydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01292"
SQ   SEQUENCE   402 AA;  43949 MW;  47FE36139DDB9342 CRC64;
     MFRLLLAFVL TLGFAQIGVA QTAETETPAA ESDRTATGGA STLEDILARQ RGEAVDNNFR
     SENTGQGNVE GLLGQFGPSG VASDSDVYRA LRFGSADVSV SSRGPADGVL IQDGGMWWLN
     FRTGPLREYG TYILGGMLAI LVLFFLIRGR IKIDGTKTGR TVTRFSSFER FGHWMFAGSF
     VILAITGLIT LYGRDFLIPL FGKEGFAVIA QGCKWLHNNL AWAFMLGLLI ITVNWIVHNI
     PNRTDLKWLA AGGGLFTKGS HPPARKFNAG QKIIFWLCVL LGISISLSGL SLLFPFEMPM
     FAKTFSVANS TGIPQMLGLS LPEQMSPHEE MQYAQVWHVM VAYVFIAIIL AHIYLGSVGM
     EGAFDAMGSG EVEEQWAREH HSLWLEEVQD KEAGKQAASP AE
//
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