ID A0A2S0MXT4_9BURK Unreviewed; 690 AA.
AC A0A2S0MXT4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:AVO40685.1};
GN ORFNames=C6571_04750 {ECO:0000313|EMBL:AVO40685.1};
OS Simplicispira suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO40685.1, ECO:0000313|Proteomes:UP000239326};
RN [1] {ECO:0000313|EMBL:AVO40685.1, ECO:0000313|Proteomes:UP000239326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1-8 {ECO:0000313|EMBL:AVO40685.1,
RC ECO:0000313|Proteomes:UP000239326};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Simplicispira sp.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP027669; AVO40685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0MXT4; -.
DR KEGG; simp:C6571_04750; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000239326; 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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 1..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 586..664
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 671..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 72932 MW; 3BE3675BE82D61A0 CRC64;
MKRILIANRG EIARRVIHTA HAMGIETVAV YSDPDANALQ VREATQAFAL GGTTSAESYL
RVDRLIEAAR ATGADAVHPG YGFLSEDAGF AQAVQDAGLC WIGPPPAAIR ALGSKSAAKA
LAAAQGVPCL PGYAGEDQSE ARFVEEAGRI GCPLMVKAVA GGGGRGMRLV QEAAQLPAAL
ASARSEAVAG FGNGELLIER AVLHPRHVEV QVFVDTHGNA IHLGERDCSV QRRHQKIIEE
APSPAVNAAL RQRMGQCAVS LAQGAGYVGA GTVEFLLEGD SFYLMEMNTR LQVEHPVTEA
LTGLDLVEWQ IRVARGEPLP LAQEGVRLEG HSIEVRLCSE DENFTPHTGR VQHFRAPAAS
AFVAVARPGE GHASLRFDHS IEAGLEVTPH YDALLGKLIV HAETREQAID AMVQALGQLE
LLGLPTNRAL LAACLEHPQF RAGDALISFL AGEAEAVREK LLKKELSAHS QYALVAILAK
NSESRGLPCS FSRPVRLRHR ESASAMAVRA LGAGHWHVQR LAGGKDGAAA DDASVLQLER
LGEHAVRCVS AGVSQRVALV PVTSQRWHLQ AGGVDWWLDD VSLRAAARAG SDAGAAELRA
PFNGRVVHVM AEVGQTLPAR GTALVIESMK LEHSLSSPAE AIVAEVLVSV GQQVTPGQVL
VRFAKSAAAV EAAPGDRQTA PKSQQPITAG
//
