ID H5X9M0_9PSEU Unreviewed; 658 AA.
AC H5X9M0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acetyl/propionyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:EHR51458.1};
GN ORFNames=SacmaDRAFT_3233 {ECO:0000313|EMBL:EHR51458.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR51458.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR51458.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR51458.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001439; EHR51458.1; -; Genomic_DNA.
DR AlphaFoldDB; H5X9M0; -.
DR STRING; 882083.SacmaDRAFT_3233; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_3_11; -.
DR Proteomes; UP000004926; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
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:UP000004926}.
FT DOMAIN 4..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 110..311
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 574..655
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 658 AA; 69040 MW; 28781CEA5816ED72 CRC64;
MTTVIENLLV ANRGEIALRV FRSCRDAGIG TVAVYSDADA DSPHATAADA AIRLPGDVPA
QTYLRAEAIV AAALAAGADA VHPGYGFLSE NADFARAVTG AGLTWVGPPA AAIESMGSKV
EAKRLMAAAG VPVLAELDPC EVTEADLPVL VKASAGGGGR GMRVVRELGE LACAVDSASA
EAASAFGDPT VFCERYLEAG RHIEVQIVAD AHGTVWAMGE RDCSIQRRHQ KVVEEAPSPL
VDEDMRQRLF ASARAAASAI GYVGAGTVEF LATGGGEFYF LEMNTRLQVE HPVTECTTGT
DLVALQLRIA EGHALPAEPP LPSGHAIEVR LYAEDPAAGW SPRSGPLYHF AVPGVTAEFT
VPRGHGIRLD SGVVDGSVVG VHYDPMLAKV IAWGPDRRST ARMLAGAVAR ARIHGVGTNR
DLLVNVLRHP AFLDGDTDTA FLDRHGIDTL AAPLATEQAV RLSVLAAALA DAAHNRARAG
VQGGLPSGWR NVVAVPQRKR YTECGANGTE HEVRYRLTRE GLQAPDYPDV TLVEAQPHRV
VLDVAGVRRA FDIARYPGLV AVDSPLGPVN LTPVPRFTDP GAELAAGSLV APMPGTVVRV
AVSRGDRVRA GEPLLFLEAM KMEHRIAAPS AGVVTQLPVS VGQQVELGAV LAVVNTEE
//
