ID A0A1E5MGS4_9MICO Unreviewed; 768 AA.
AC A0A1E5MGS4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Formate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Cus16_2532 {ECO:0000313|EMBL:OEI67782.1};
OS Curtobacterium sp. ER1/6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1891920 {ECO:0000313|EMBL:OEI67782.1, ECO:0000313|Proteomes:UP000095245};
RN [1] {ECO:0000313|EMBL:OEI67782.1, ECO:0000313|Proteomes:UP000095245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER1/6 {ECO:0000313|EMBL:OEI67782.1,
RC ECO:0000313|Proteomes:UP000095245};
RA Garrido L.M., Alves J.M., Oliveira L.S., Gruber A., Padilla G.,
RA Araujo W.L.;
RT "Draft genome sequence of Curtobacterium sp. strain ER1/6, an endophytic
RT strain isolated from Citrus sinensis with potential to be used as a
RT biocontrol agent.";
RL Submitted (AUG-2016) 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 -!- 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:OEI67782.1}.
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DR EMBL; MJAK01000008; OEI67782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5MGS4; -.
DR STRING; 1891920.Cus16_2532; -.
DR PATRIC; fig|1891920.3.peg.3093; -.
DR Proteomes; UP000095245; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000095245}.
FT DOMAIN 120..496
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 648..753
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 768 AA; 84035 MW; BB18C118940C0C1F CRC64;
MTEQPPKDDV TDAEMTVGEP KEWAAGVPGV LHSMTPAIEQ LGVARTAKLM LNLNQKGGFD
CMSCAWPDPD KRKTAEFCEN GAKAVVWEAT PVLVPRSFWA EHSVDDLADK TEYWLGMQGR
ITEPVWKPAG KDHYQPVSWE RAFRIIADKL NGLDSPDQAS FYTSGRTSNE AAFVYQLFVR
AFGTNNLPDC SNMCHESTSL AMAEVVGIGK STIAYDDFEE TELIIVMGQN PGTNHPRMLT
ALEDAKENGA EIVAVNPLPE SSLKRYKNPQ KVRGVVGRGT EIADQFVQIR LGGDMALLQA
LSKRVVQAEL AAPGTVVDHA FIAEHTSGYE AFVEHVLQVD DDEVVRATGL TLEEIDELAE
RYMRSERTII TWAMGITQHT KAVDTIKEII NLLLLRGNIG RPGAGASPIR GHSNVQGDRT
MGIWEQMPDS FLDALAKEFH FEPPREHGVD ALKGITAMQR GEITFWMGMG GNLVAAISDS
QLAEAAFRGT EMTVQVSTKL NRSHAVVGDE ALILPTMGRT EIDVQAAGPQ FVSVEDTVCS
VHGSHGQVPP VAPGLLSEVA IVCELAKATL GDRVAVDWQG MRDDYDVIRD HISHVVPGFE
DYSRRAASKE GFVLPNGPRD SRSFGTKTGK AMITVNELEH VERPEGTLLL QTLRAHDQYN
TTIYSLNDRY RGIKKGRHVV FVNPDDLTEL GLQDGDRVDV ATVWDDDVER VLRDYRVVAY
PSARGCAAAY FPEANVLVPL DSAAKGSNTP VSKAVPVRLT RVAVPAGV
//
