ID H0Q4M3_9RHOO Unreviewed; 879 AA.
AC H0Q4M3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:BAL26936.1};
GN ORFNames=AZKH_p0053 {ECO:0000313|EMBL:BAL26936.1};
OS Azoarcus sp. KH32C.
OG Plasmid pAZKH {ECO:0000313|EMBL:BAL26936.1,
OG ECO:0000313|Proteomes:UP000007106}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL26936.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL26936.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL26936.1,
RC ECO:0000313|Proteomes:UP000007106};
RC PLASMID=Plasmid pAZKH {ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) 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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; AP012305; BAL26936.1; -; Genomic_DNA.
DR RefSeq; WP_015451713.1; NC_020548.1.
DR AlphaFoldDB; H0Q4M3; -.
DR KEGG; aza:AZKH_p0053; -.
DR PATRIC; fig|748247.4.peg.4625; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_9_0_4; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000007106; Plasmid pAZKH.
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; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
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 Pfam; PF10518; TAT_signal; 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; PS51318; TAT; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:BAL26936.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007106};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 48..105
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 879 AA; 98502 MW; 1E7BBC2232818C48 CRC64;
MEFPKITRRT FLKASAGTTA AAATAPRLLH AMENELGGKD FDPVNAAERK AIPINCHVCN
IQDGAIAYVE NDRVVKLEGN PEHVSTRGRL CAKGNSGMWY SYDPDRILYP LKRVGARGEG
KWKRITWDEA LAEVAQKLDA ALKEDPNTIM MKYGRNRTGG TLDRFMQTLG SATVVNHTSV
CESSKKVGME PTWGPDIETP DFANAKYVLN FGSNVLEAAY FHNPLSQRVT EGRIDNQMKI
VTFDVRLSNT AGFSDEWIPV FPATDGAVAL SIGHVILRED LQDSDFINTW TNVTVDELKA
HYAQYTPEWA SKISGVPVAT IERIAREFAT TKPATLFTYR GPAKHLYGSY NEKACMMLPI
MTGNVEKRGG YCLPRGMGWP QPEPQPGKPV KASYLAHPPD YPLAAHKVSH LVPFWIAEGK
QKINVYFTYQ DNPVYTNPGS MAVWGKLYKD EKLIPYFVSM SPFMGEETAL ADLILPDCPY
LERWEPESMP NSLWPWLGIR QPVHKSLGES RENRVMLRDI IWKLDPDGSR GMKKFWDFKD
GEDYMRHHFD NVPGLKEAGG LDFLKKHGVW PIYGKLDPRT GKVTDKTGRE IQAEYGLYRK
ELSAADMEGA MVDARGLITK NGKAIGIRRN GKNHVGFPTG NRLINVRVDE WAEYGFNPMP
TFKRIPWHET MSDDEMILST FKLNVHKQSR TAAVKWLAEI AHSNPAWMNP ETAKKLGVKT
GDLVRIESAV GYLVTKAYVT EGIHPKVVSI PTGFGHWEYG RLATLRLKDK KGDASHGQDD
PDLNNVWWDD RGVHPNNIIP VVADPIGGSQ GWFDTVVKVT KAGPNDKYGD TQGDWDKHVA
AFKETMRYAY TGDLHRKMHP EMAAWAGPDS VKKKAPGGH
//