ID A0A1G5PTI7_9GAMM Unreviewed; 963 AA.
AC A0A1G5PTI7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:SCZ52389.1};
GN ORFNames=SAMN03097708_00741 {ECO:0000313|EMBL:SCZ52389.1};
OS Thiohalomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalomonadales;
OC Thiohalomonadaceae; Thiohalomonas.
OX NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ52389.1, ECO:0000313|Proteomes:UP000199648};
RN [1] {ECO:0000313|EMBL:SCZ52389.1, ECO:0000313|Proteomes:UP000199648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLD2 {ECO:0000313|EMBL:SCZ52389.1,
RC ECO:0000313|Proteomes:UP000199648};
RA de Groot N.N.;
RL Submitted (OCT-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; FMWD01000002; SCZ52389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5PTI7; -.
DR STRING; 415747.SAMN03097708_00741; -.
DR Proteomes; UP000199648; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02783; MopB_CT_2; 1.
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; 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 PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 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:UP000199648}.
FT DOMAIN 13..69
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 963 AA; 108495 MW; 4DF2AB1F4234FD99 CRC64;
MSDMAKNATE GRTEVKNTTC YMCACRCGIR VTLRDGEVRY IQGNPDHPLN KGVICAKGSS
GIMKQYSPAR LTRPLKRKAG ADRGDAQFEP ISWDEAFGML EERLAHIRET DPKKFALFTG
RDQMQALTGL FAKNFGTPNY AAHGGFCSVN MAAGMIYTIG GSFWEFGGPD LDRAKLFVMI
GTAEDHHSNP MKMALSKFKR NGGRFISVNP VRTGYSAIAD EWIPIKPGTD GALMLALTHE
IIKTGLYDRE FLIQYSNAAE LVNLNEESPE HGMFVRFEVP PEEGCFDPQN KLWWDRELNK
PISTHTPGAD PYLLGDFRLS DGTPVKPSFQ LLKERVEEYT PEWAADITGI PAETIRRLAH
EMGITARDEK IELPIAWTDT WGNEHQSVTG NPVAFHAMRG LAAHSNGFHT IRAMSILMSI
LGTIDRPGGF RHKAPFPRPI PPCPKTPTGP EDVKAGQPLN GMPLGWPADP DDLFVDDKGQ
PVRIDKAFSW EHPLSVHGMM HNAITNAWRG DPYSIDTLLI FMANMSWNSS MNTDEVRKML
NDKDENGEYK IPFLVVADAF QSEMVAYADL VLPDTTYLER HDVMSMLDRP ISEFEGPVDS
VRIPVVPPKG ECKPFQEVLI ELGSRLKLPP FTHEDGSRKF RDYPDFVTNF ETAPGSGIGF
LAGWRGKGGE KSIRGEPNPN QWEMYAKNNC VFQHELPKSY QYMRNWNQGY LQWAQEHGMT
RYAEPINVHI YSEVLQKFRL AAQGKTQGKQ PPDNLRRRID LFFDPLPFYF EPLESQLSDK
QAYPLNAITQ RPMAMYHSWD SQNAWLRQIH TYNFLHLHPK TAEAAGIEDG GWMWVESMHG
KVRCMARYSE AVEPGTVWTW NAVGKASGAW NLDDDANEAR QGFLLNHVIA EELPAHDAGK
HISNSDPVTG QAGWYDVRVR VYPAGPDEEK VSWPQFTPMP QVPGTGERRP WLNYVAGLFE
KRG
//