ID A0A3N4Z2R2_9MICO Unreviewed; 1100 AA.
AC A0A3N4Z2R2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:RPF27539.1};
GN ORFNames=EDD32_2027 {ECO:0000313|EMBL:RPF27539.1};
OS Georgenia muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=154117 {ECO:0000313|EMBL:RPF27539.1, ECO:0000313|Proteomes:UP000280726};
RN [1] {ECO:0000313|EMBL:RPF27539.1, ECO:0000313|Proteomes:UP000280726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14418 {ECO:0000313|EMBL:RPF27539.1,
RC ECO:0000313|Proteomes:UP000280726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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}.
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:RPF27539.1}.
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DR EMBL; RKRA01000001; RPF27539.1; -; Genomic_DNA.
DR Proteomes; UP000280726; Unassembled WGS sequence.
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; 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.
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:UP000280726};
KW Selenium {ECO:0000313|EMBL:RPF27539.1};
KW Selenocysteine {ECO:0000313|EMBL:RPF27539.1}.
FT DOMAIN 44..100
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 335..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 190
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:RPF27539.1"
SQ SEQUENCE 1100 AA; 121673 MW; 69F227FC8FA2ED75 CRC64;
METSKVFLSW PVLRQLTGTD PLGRGPAVRS ARTERLTART ETADRVARSV CPYCAVGCGQ
RVYVKDDKVV QIEGDPDSPI SRGRLCPKGS ASKNLVTSPL RLTKVRYRRP YGTQWEDLDL
DVAMGMIADR VVDARRRTWQ DRDEEGRYVH RTLGIASLGG ATLDNEENYL IKKLFTALGA
LQIENQARIU HSATVPGLGT SFGRGGATGF QQDLVNADCI IIQGSNMAEA HPVGFQWVVE
AKARGARVIH VDPRFTRTSA LADTYVPIRV GSDIVFLGAI VNHVLSNGLD FREYVLAYTN
AATIVSEDYL DTEDLDGLFS GFDPDTRTYD SASWQYAGSE GAGDGEGEEA RDRATARGME
HETHGMQVPA EVQRDETLQH PRTVYQILRR HFARYTPEVV EEVCGISREQ FLDVANAWAA
SSGRERTTAL VYSVGWTQHS VGAQYIRTGA ILQLLLGNMG RPGGGILALR GHASIQGSTD
IPTLFNLLPG YLPMPRAQDH PDLQSWVGEM RPATAKGFWS MSRAYAISLL KAYWGPAATA
ENDFAYDYLP RLTGDHGTYR TVLDMIDGKV KGYFLLGQNP AVGSAHGKAQ RLGMANLDWL
VVRDLYEIES ATFWRDSPEI ETGEIVPEQC RTEVFLMPAA SHVEKEGTFT QTQRLLQWRE
KAVDPEGDRR SELWFFYHLG RLVRERLAGS TEDRDRPVLD LAWDYPTHGD EPSAEAVLRE
INGYEVATGR PLSTFTELRD DGTTVGGCWI YTGVLADGVN QAARRRPGSE QSWVAPEWGW
AWPANRRILY NRASADPQGR PWSERKAYVW WDEDAGRWTG HDVPDFEAAK PPGYRPPPGA
TGVEAIAGDD AFIMQGDGKG ALFVPSGLVD GPLPTHYEPV ESVVRNALYG QQSNPTRVQY
RRPDNPMHPL DDAVFPYVFT TSRLTEHHTA GGMSRFLEYL SELQPEMFVE VSPQLAAERG
LAHLGWCHVV TARAAVEGRV LVTERLRPLR IEGRTVHQVW LPYHWGSGGL VTGDAANDLF
GITLDPNVLI QETKAGTCDV RAGRRPRGRA LLQLVDDYRR RAGTDVDRPI VTASPSAVTR
SHGVGGTGEP DDTDGGDDGR
//
