ID K6YU42_9ALTE Unreviewed; 726 AA.
AC K6YU42;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:AGH44881.1};
GN ORFNames=C427_2772 {ECO:0000313|EMBL:AGH44881.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH44881.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH44881.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH44881.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP003837; AGH44881.1; -; Genomic_DNA.
DR AlphaFoldDB; K6YU42; -.
DR STRING; 1129794.C427_2772; -.
DR KEGG; gps:C427_2772; -.
DR PATRIC; fig|1129794.4.peg.2756; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000011864; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR CDD; cd02782; MopB_CT_1; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011864}.
FT DOMAIN 9..65
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 726 AA; 80291 MW; 7EA9E91FC17EEC7B CRC64;
MTLIMPTEKQ KHYSTCTLCE AMCGIEVTTQ DRNILSIVGD KANPFSEGHV CPKAMALKDL
YEDPERIRTP IEKTAEGGWQ EVSWDYALDK VATNLFDIQQ KHGVESVATY LGNPNAHNMG
SILFGPYFYR SLKSHNRYSA TSVDQLPHHI VSRQLFGHQS QIPIPDIDHT QHFMIIGGNP
LASNGSIMTV PHIKRRLKAI QARGGKVVVI DPKKSETADM SSEHHFIKPG TDALLMLAMI
HTLFDKQLIA ADALLGFAAD LLSVEKYVVD YPPKRVANLT GMSESQIIAL VESFCAAGPA
VCYGRMGASV QAFGTLTQYL IMLFNMLTGN LDRQGGMMFT QPAADLLPHS GRGSIANFFT
RVRNLPAFAG EFPVSALAEE MLTDGEGQIK AIVIGAGNPI LTTPNGQQLD KAFENLDFVV
AVDFYITETS RHADIILPPV TALERDHYDI VFHNFAVRNS TKFSPAIFPP AETTKTDWQI
YLGLAERLDK LNGLPTDKYQ TLWQKEPKGV VDDLLKSGRY RHEGEVLSID LLLKKPHGID
LGPLQPDLPE AIYHNDKKID LSFDYFMADL TRLDKHFFAS EFSISEASGL ATDESLQLIG
RRHLKTNNSW LHNSQRMVKG TNNGWSRCTA QIHPDDASKH NIQDQQLITV TSRVGKVTLP
AEITEKIMPG VISIPHGWGH NKKGSQWHTA EQHAGVSVND LTDEMVIDEL SGNAVLNGVP
VTIEAA
//
