ID A0A1C4YP11_9ACTN Unreviewed; 1098 AA.
AC A0A1C4YP11;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SCF22400.1};
GN ORFNames=GA0074696_3557 {ECO:0000313|EMBL:SCF22400.1};
OS Micromonospora purpureochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47872 {ECO:0000313|EMBL:SCF22400.1, ECO:0000313|Proteomes:UP000198228};
RN [1] {ECO:0000313|EMBL:SCF22400.1, ECO:0000313|Proteomes:UP000198228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43821 {ECO:0000313|EMBL:SCF22400.1,
RC ECO:0000313|Proteomes:UP000198228};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LT607410; SCF22400.1; -; Genomic_DNA.
DR Proteomes; UP000198228; Chromosome i.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-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:0045333; P:cellular respiration; IEA:InterPro.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR048158; Formate_DH_Act.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR NCBIfam; NF041513; formate_DH_Act; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 2.
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.
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 Selenium {ECO:0000313|EMBL:SCF22400.1};
KW Selenocysteine {ECO:0000313|EMBL:SCF22400.1}.
FT DOMAIN 44..100
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 334..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 190
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:SCF22400.1"
SQ SEQUENCE 1098 AA; 121161 MW; BDE578B6579E0FC1 CRC64;
MGLRTFIEGW PVYRQLTGTD PLGRGAAAQS GRSAELTART ETADSMARSV CPYCAVGCGQ
RVFVTDGRVT QIEGDPDSPI SRGRLCPKGS ASKSLVTSPL RQTTVRYRRP YATEWEDLEL
DTALDMIADR ILAAREETWE DVDSEGRPLN RTLGISSLGG ATLDNEENYL IKKLFTAMGA
LQIENQARIU HSATVPGLGT SFGRGGATDF QQDVANADVI VIQGSNMAEA HPVGFQWVME
AKRRGAKVFH VDPRFTRTSA VADTYLPIRA GTDIALLGGV VRYILENELD FREYVLAYTN
AATIVSERYV DAEDGDGFFS GFDPETSSYV QDSWQYEGHE GTSGSGHTAK ERDSAAGLRH
ESHGAQVAGQ VPRDETLQHP RCVYQILKRH FARYTPEMVE RVCGIPQERF LELARAWTEN
SGRERTGVLI YSVGWTQHSV GVQYIRTGAI IQLLLGNMGR PGGGILALRG HASIQGSTDI
PTLFNLLPGY LPMPHHADHP TFDQWVDSIR HPGQKGFWGN ARAFGASLLK AYWGEAATPE
NDFCYGYLPR MTGDHGTYQQ VLNMIDGKVK GYFLLGQNPA VGSAHGRAQR LGMANLDWLV
VRDLFMIESA TFWKNGPEVA TGEIVPQECR TEVFFLPAAS HVEKEGTFTQ TQRLLQWREK
ALDPPGDARS ELWFFYHLGC RLREKLADSD QPRDRALLDL AWDYPTHGPH AEPSAEAVLR
EINGYDVATG RPLSAFAEAR DDGSTAIGCW IYTGVYADGV NQAARRKSRH EQDWVAAEWG
WAWPANRRTL YNRASADPQG RPWSERKRYV WWDPDAGEWT GYDVPDFEKT KPPTYRPPEG
ASGPAGIAGD DPFVMQPDGK GWLYAPSGVL DGPLPTHFEP AESPLRNPLY GQQANPIRKV
YDHPVNSVNP SPPEEHSQVF PYVFTVSRLT EHHTAGAMSR TVRPLAELQP EMFVEVSPEL
AAETGVTHLG WAHLVSGRAV IEAKVLVTDR LTPLRVDGRV IHQIWLPYHF GFEGLVTGDS
ANDLFGITLD PNVLIQESKV GTCAVRPGRR PTGPALRDLV ADYQRRAGIV PGRSAPTVTD
GVRPPAPPPG EGEDVDDA
//
