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Database: UniProt
Entry: A0A0J1GJR0_9GAMM
LinkDB: A0A0J1GJR0_9GAMM
Original site: A0A0J1GJR0_9GAMM 
ID   A0A0J1GJR0_9GAMM        Unreviewed;      1395 AA.
AC   A0A0J1GJR0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KLU99919.1};
GN   ORFNames=ABT58_15820 {ECO:0000313|EMBL:KLU99919.1};
OS   Photobacterium aphoticum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU99919.1, ECO:0000313|Proteomes:UP000036426};
RN   [1] {ECO:0000313|EMBL:KLU99919.1, ECO:0000313|Proteomes:UP000036426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU99919.1,
RC   ECO:0000313|Proteomes:UP000036426};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC       molybdopterin-containing oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00007023}.
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:KLU99919.1}.
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DR   EMBL; LDOV01000027; KLU99919.1; -; Genomic_DNA.
DR   RefSeq; WP_047875377.1; NZ_PYMF01000023.1.
DR   PATRIC; fig|754436.4.peg.3354; -.
DR   OrthoDB; 9810782at2; -.
DR   Proteomes; UP000036426; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR   CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR   CDD; cd02753; MopB_Formate-Dh-H; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041925; CT_Formate-Dh_H.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR041924; Formate_Dh-H_N.
DR   InterPro; IPR006478; Formate_DH_asu.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43742:SF2; ASSIMILATORY NITRATE REDUCTASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036426}.
FT   DOMAIN          1..77
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          611..640
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          662..690
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          699..757
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1395 AA;  152433 MW;  D7C95F098A33D98C CRC64;
     MNNVIIDGQS IAVDGQQSLL DVANAHQIEI PSLCGLNKSG EKVPCDLCMV EIDGQGMQRA
     CEVTAQAGMS VTTQSDALSA HRRQALNRIM ADHYADCEAP CQTACPAGVD IQSYLYHIAQ
     NDHQKAVEVI KRTLPMPLSI GRVCPAFCEA ECRRGIVDEP LAIRQLKRHA ADIDLEAQEQ
     YVPPRKADKG KRVAIIGSGP GGLSCGYYLS NEGYAVTVFE SMPKAGGWLR YGIPEYRLPK
     AILDKEIELI CRNGMEVKTN QSLGKDMQLS ELVADYDAVC LAVGASQAVE MHYTGSDLDG
     CYLGVDYLKD YVTDKQYTTG KKVAVIGGGN TAIDCARTAV RDGADTTLIY RRTRDEMPAE
     DYEIAEAEHE GVKFHFLTNP VENMADENGR VTDVKLEKMA LGEPDASGRR SPVPTGEYVV
     EHFDTVISAV SQKPDLSFLN DDTLELPITR WQTVESCEHT MHVGVENIFS IGDLRRGPAT
     AIEAVADGRV AAHAIDRYLH GDMAAVPVKP FNAQKAASVK QVDPAQFAGI QKAMRAIMPE
     LTTAERELSF AEVETGFDNE DAMREAARCL ECGCQANTDC KLRDYSTEYK AEQNAEAMAD
     CQKFAVDNSA EFIVFDANRC ISCGQCVQTC NEKTVHGVLS FMKNEDGTSA NRPECRPGFD
     NRQPMGDSNC VQCGACVQVC PTGALVDGRD RSQGRIEMLT PVDTICTYCG VGCKVTMFVD
     EATNKIRYVQ GAKSSPVNQG MLCVKGRFGF DFIQSEERLT HPLIRRGGRN GKLEKATWSE
     AIALVADKLG EIKATHGGNA LAGFSSAKTT NEDNFAFQKF FRRELLTNNI DHCARLCHST
     TVTGLEASLG SGAMTNDIPS IQHSDLIFII GSDTTAAHPI IASHIKQALR AGKARLVVAD
     PKHVEIADHA SLYVAHRPGT DVMLLNGIMQ QIIKNGWQDE AYIAERVTGF DVLKDEVMRE
     DYSPANVELI TGVKQADLLH MAEMIGTAER TAVYYSMGIT QHTTGHDNVR SIANLQMLCG
     NIGIEGGGIN PLRGQSNVQG ACDMGALPKD FPGYQKIRNP EAHQKFAKAW DCPELPAEDG
     LTLTEIVDAA CQQQVRGLYV MGENPVLSDP DQKHVLEALA TLDFLVVQDI FLTETAQLAD
     VVLPSFSFAE KSGHFTNTER RVQRVSPALR APGEAMEDWR IIQTIANAMG SDWAYESVRD
     ITDEINVLTP QYAGITWDRV GAEGIQWPCP STEHAGTRIM HKDSMMRGKG EMAAVPFRYA
     AELPDPEYPM VLTTGRLLEQ FHTGTMTRKT KGLDNLAGPR AMISVQDAER LGISNGEMLK
     VSTRRGSIET PAFVTKRMQE GVIFVPFHFV ESAANKLTVT ATDPHAKIPE FKVAAVKIEK
     AHVAETEAEA EILPA
//
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