ID A0A0D6PCS9_9PROT Unreviewed; 571 AA.
AC A0A0D6PCS9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:GAN79136.1};
GN ORFNames=Aam_017_041 {ECO:0000313|EMBL:GAN79136.1};
OS Acidocella aminolytica 101 = DSM 11237.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN79136.1, ECO:0000313|Proteomes:UP000032668};
RN [1] {ECO:0000313|EMBL:GAN79136.1, ECO:0000313|Proteomes:UP000032668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:GAN79136.1}.
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DR EMBL; BANC01000017; GAN79136.1; -; Genomic_DNA.
DR RefSeq; WP_048877601.1; NZ_FQVJ01000006.1.
DR AlphaFoldDB; A0A0D6PCS9; -.
DR STRING; 1120923.SAMN02746095_00970; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000032668; Unassembled WGS sequence.
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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
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; 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; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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; 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:UP000032668}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 571 AA; 60969 MW; 1254C4749599A528 CRC64;
MKTVLIANRG EIAVRIIRAC HDYGLRAVAA YADPDEDSLF VRLADEAYAL HGTSAAETYL
DIPKLLAIAK RAGADAVHPG YGFLSERAVF ARAVQAEGLT WIGPDPAVIA ALGDKISARD
IAQSVGAPLA AGSDGPVDSA ASALAFARQH GLPLAIKAAH GGGGRGLKVV RVLEEVEEQY
ASAVREAEAA FGRGECFLER FLDKPRHIEV QIIADKHGNV VVLGTRDCSL QRRNQKLVEE
APAPFLTPSQ RDEIEDAARR ICQAAGYSSA GTVEFLLGQD GTLSFLEVNT RLQVEHPVTE
QTTGIDLVIE QFRVAEGLKL SIPNPPPAMG HAIEFRINAE DAAKGFLPTP GRITLFEPPS
GPGVRLDSGV VTGSLIPGQY DSLAAKLIVT GSTRAEALRR ARRALAEFTI EGVATVLPFH
RAVLEHPSFT GENGFGVYTS WIETEFQPAL TPAPRPALLE DDTLLRLPLE IDGRRHQIGL
PRALLNRLGQ SAPAPTPPST QDNSTLYAPV AGHLQGWKVE DGAEVQEGDL LAVMEAMKME
VRITSPRAGC FQQAVKTGAF LEAGAALGRF A
//
