ID Q729X1_DESVH Unreviewed; 471 AA.
AC Q729X1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase, putative {ECO:0000313|EMBL:AAS96699.1};
GN OrderedLocusNames=DVU_2226 {ECO:0000313|EMBL:AAS96699.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS96699.1, ECO:0000313|Proteomes:UP000002194};
RN [1] {ECO:0000313|EMBL:AAS96699.1, ECO:0000313|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000313|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- INTERACTION:
CC Q729X1; Q729X3: DVU_2224; NbExp=4; IntAct=EBI-10067436, EBI-10067439;
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DR EMBL; AE017285; AAS96699.1; -; Genomic_DNA.
DR RefSeq; WP_010939501.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_011439.1; NC_002937.3.
DR AlphaFoldDB; Q729X1; -.
DR SMR; Q729X1; -.
DR IntAct; Q729X1; 3.
DR STRING; 882.DVU_2226; -.
DR PaxDb; 882-DVU_2226; -.
DR EnsemblBacteria; AAS96699; AAS96699; DVU_2226.
DR KEGG; dvu:DVU_2226; -.
DR PATRIC; fig|882.5.peg.2021; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_7; -.
DR OrthoDB; 9769961at2; -.
DR PhylomeDB; Q729X1; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000002194}.
FT DOMAIN 4..471
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..347
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 471 AA; 53303 MW; EC40657D1EDAAC31 CRC64;
MQTNDHKVLV ANRGEIATRI VRACHRLGLE FTCVYTAEDA ASGHVRLARE LGGANSLYRV
SSYHDANELL AVADDAGCTA VHPGYGFFAE DYRFARRVAQ RERKLIFIGP SWRVIRELGD
KINTKRLARS LGVPTVPGSD KPIYDELEAE KVAQSLYEFQ EQQGIRRPLV LVKASAGGGG
MGIEEVYDLD LFKSVYRRIR NYALRQFKDE GVLIEQRIRD FNHLEVQIVS DRTGRNPVHF
GTRNCSIQSI GLQKRIEVAP GFDPTSIEYG FDAAQVLRDI TYHSLAMARK VGYDNVGTWE
WIVTRDGHPF LMEVNTRIQV ENGVSARIAR VNGQEVDLIA EQIRIGLGQP LGYGQEDITF
EGVGIEYRLI AEDPDNRFTP WVGRIDAFGW PEEDWARMYT HVPTEEPYDI PTEFDPNLAL
AIIWGKDLEE VKRRGVSFLE GLTLQGQNKA GDELRSNVNF LRDNTGRILR F
//
