ID A0A0Q6Z9C5_9BRAD Unreviewed; 1106 AA.
AC A0A0Q6Z9C5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:KQW20488.1};
GN ORFNames=ASC80_09510 {ECO:0000313|EMBL:KQW20488.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW20488.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW20488.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20488.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW20488.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20488.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW20488.1}.
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DR EMBL; LMDP01000002; KQW20488.1; -; Genomic_DNA.
DR RefSeq; WP_056296036.1; NZ_LMDP01000002.1.
DR AlphaFoldDB; A0A0Q6Z9C5; -.
DR STRING; 1736436.ASC80_09510; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000051348; 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; IPR034733; AcCoA_carboxyl_beta.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF5; BLL7292 PROTEIN; 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; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 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:UP000051348}.
FT DOMAIN 2..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 491..569
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 849..1088
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1106 AA; 117702 MW; EEA5D8463350BA61 CRC64;
MSFRKLLIAN RGEIAIRIAR AAADAGLASV AVYSADDALS LHVRAADEAR EIPGRGARAY
LDIEGVIAAA KAAGCDALHP GYGFLSENAD LARRCAEEKI VFVGPNPSAL QLFGDKVEAK
ALAKRCGVPI IEGTVGPTTL DEAKTFFASL GKGGAVMIKA MAGGGGRGMR IVEDASKLEE
AYARCQSEAK AAFGSAGVYV ERLIRKARHI EVQIIGDRHG AVSHLWEREC TIQRRNQKLI
EVAPSPSLSD ELRERIVDAA KQLAAAANYD SLGTFEFLVD GEVAGDESAF AFIEANPRLQ
VEHTVTEEVL GIDLVRSQLA VAAGATLASL GLNQAAVPAP RGYAMQLRVN MEVMDEQGQT
KPTGGVLAVF DPPSGLGVRI DTFGYFGYKT SAAFDSLLAK VIVHASVAQW ADVVAKASRA
LREFRIGGVA TNIPFLQAVL AHPDFIANRI STSFVDSHVA ALVGAAKETA PPLFFSNDSA
MDGNGDAEKF AGPAVGPAGS ESVAAPLQGT VVVIEVAEGD LVRPGQQIAV IESMKMEHLV
TAPHGGKVTK IAAGDGVTLM QGDPIVFIEP AEVGGHDAEE ETEVDLDHIR ADLAENIARH
ANTLDENRPA SVARRRKTNQ RTARENIAQL VDDGSFVEYG SLAIAAQRRR RALDDLIKNT
PADGLITGVA TVNADKFGEQ GARCMVISYD YTVLAGTQGH MNHKKIDRML GLAEQWQMPL
VFYAEGGGGR PGDTDRLGMT GLDGPSFVQF AKLSGLVPVI GVVSGYCFAG NAAMLGCCDV
IIATKNASIG MGGPAMIEGG GLGVYHPAEV GPVSFQSPNG VVDILVEDEE EATAAAQKYL
SYFQGAVTDW KAPDQRLLRR AIPENRLRVY DIRTVIDLLA DEGSVLEIRR DFGVGMITAF
IRIEGKPFGL IANNPKHLGG AIDANAGDKA ARFMQLCDAF DIPIVSLCDT PGFMVGPEAE
KTAIVRHVAR MFVTGASLTV PLFGVVLRKG YGLGAQSMIG GGFHASFFTV AWPTGEFGGM
GLEGYVRLGF RKEMEAIADP VEREAYYKDK VAQLYANGKA VSIASVLEID EVIDPAETRN
WIMAGLRSMP KPAPRDHRKR PCIDTW
//
