ID A0A1V1W7J5_9ACTN Unreviewed; 802 AA.
AC A0A1V1W7J5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carbon monoxyde dehydrogenase large subunit {ECO:0000313|EMBL:GAW56220.1};
GN ORFNames=PD653_3656 {ECO:0000313|EMBL:GAW56220.1};
OS Nocardioides sp. PD653.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=393303 {ECO:0000313|EMBL:GAW56220.1, ECO:0000313|Proteomes:UP000194147};
RN [1] {ECO:0000313|Proteomes:UP000194147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD653 {ECO:0000313|Proteomes:UP000194147};
RA Ito K., Takagi K., Tanaka N., Kanesaki Y., Iwasaki A.;
RT "Nocardioides sp. PD653 draft genome sequence.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:GAW56220.1}.
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DR EMBL; BDJG01000039; GAW56220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1W7J5; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000194147; Unassembled WGS sequence.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012780; CO_Mo_DH_lsu.
DR NCBIfam; TIGR02416; CO_dehy_Mo_lg; 1.
DR PANTHER; PTHR11908:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000194147}.
FT DOMAIN 40..149
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 86179 MW; 81C45F073F149187 CRC64;
MTTLDEGVAA TPEDLDHADN DQHPVGHGRM LRKEDPRFIR GMGKYVDDLQ LKGMLHLAIL
RSPVAHATIV SIDTTAAQAH PKVKAVITGA DLAAQGLAWM PTLSNDVQAV LATDKVRFQG
QEVAFVVAED RYSARDALEL IDVEYDILPP VVDVRTALAP DAPVIRTDLE GKTDNHCFDW
ETGDKAATDA VFARADVVVT EDIVYPRVHP APMETCGCVA DYERVSGQLT LWTTSQAPHA
HRTVYALVAG LPEHKIRVIA PDIGGGFGNK VPIYPGYVCA IVASLVIGKP VKWMEDRSEN
LVSTGFARDY VMRGEIAATK EGKILAIRTH VIADHGAFNG TAAPTKYPAG FFGVFTGSYD
LEAAYCSMTA VYTNKAPGGV AYACSFRITE AVYLVERLVD CLAYDLEKDP VELRRQNFIQ
PEQFPYTTKT GWVYDSGEYE RALDLALEMA GYDELRAEQA EKRERGELMG IGVAFFTEAV
GAGPRKDMDI LGLGMADGSE LRIHPTGKAV LRVSCMSQGQ GHETTFAQIV AEEIGIPPAD
IQVINGDTDQ TPFGLGTYGS RSTPVSGAAA ALVSRKVRDK AQIIASGMLE VSVADLEWQK
GSFAVKGDPS RSVTIQDIAM RAHGAGDLPD GVEGGLEAQI CYNPENLTYP FGAYICVVDI
DPGTAAVKVR RFVAVDDCGT RINPMIIEGQ VHGGLTDGVG MALMEMIAFD DEGNCLGGSL
MDYLIPTALE VPHWETGHTV TPSPHHPIGA KGVGESATVG SPPAVVNAVV DALKPFGIRH
ADMPLTPSRV WDAMQGRPTP PI
//
