ID A0A160FLL9_9BURK Unreviewed; 1020 AA.
AC A0A160FLL9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:ANB73036.1};
GN ORFNames=AYM40_12175 {ECO:0000313|EMBL:ANB73036.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB73036.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB73036.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB73036.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
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DR EMBL; CP014578; ANB73036.1; -; Genomic_DNA.
DR RefSeq; WP_063496445.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FLL9; -.
DR STRING; 1804984.AYM40_12175; -.
DR KEGG; buz:AYM40_12175; -.
DR Proteomes; UP000076852; Chromosome 1.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05018; CoxG; 1.
DR Gene3D; 3.30.530.20; -; 1.
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; IPR010419; CO_DH_gsu.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF06240; COXG; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF55961; Bet v1-like; 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:UP000076852}.
FT DOMAIN 46..157
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 109003 MW; 5326E5415A39D6F1 CRC64;
MNQRDTVAEL VADARPAGEP ETSAERQRQR HVGRSMERVE DPAILTGRGR YGDDIAVKPG
TLHAAVLRSP HAHAELRSID TDAALKLAGV RAVLTRDDLP GWSRPFVVGV KSPMEQWALA
MDRVRYVGEP VAVVLAESRA LAEDALDLIK VEYQTLPPVT SIENAIADDA PVLHPKVGTN
VISDRHYRYG EPEAAFERAP HRVTIDAHYP RNTCAPIECG VVIAEYLSGD EGYDVTSNFM
GPFSLHAVMS MALNVPANRL RHKAPRDSGG SFGVKQAVFP YVVLMCLASR KAGAPVKWVE
DRLEHLSAAT SATARLTTLE AAVEGDGRIT ALSYDQIEDC GGYLRAPEPA TFYRMHGCLT
GAYAIPNLVV RNRVTLTNKT PTGLVRGFGG PQVYFALERL MQRIAIELKL EVLDVYRRNF
VAAEAFPYRA AAGALLDSGN YQEALRRSLA EGGYDELVAR RDAARREGRV YGIGFAAIVE
PSVSNMGYIT TVMPAEARKK AGPKSGAIAS ATVSVDLLGG VVVTIASTPA GQGHMTVCAQ
VVADVLGLNP RDIVVNVEFD THKDAWSVAA GNYSSRFAGA VAGTVHLAAM RVRDKVARIV
AKQSGCAPED ICFEDGRIFA KGKEDRALPF GRVASNAPHW APALLPEGEE PGLRETVFWT
PPHMDAPDEQ DRINTSAAYG FAFDMCAVEV DRATGRVRID RYVTAHDAGT LLNPALADGQ
IRGAFAQGLG AALMEEFRYG ADGSFQSGTL ADYLMPTTCE VPDPVIVHLE TPSPFTPLGA
KGLGEGNNMS TPPCIANAVA DALGVEDIRL PLTPAKVMHL IGIDDPPPSR PELLQAAAAA
ASNKALAGGK ALTARGTVDL DATPEAIFAV LMDPQALAKV IPGCHALEAT GPNQYRADVT
VGVGMIKARF EARIGLSDID APHRLRLAGA GSSPLGTARG EGLVELTPTE RGTRLSYDYE
AQVSGKVAAV GGRMLEGAAK VVLRQLFESL GRQASGKPVD QGRAQGSWLS RFLAFFRSRT
//
