ID Q5L8U5_BACFN Unreviewed; 1073 AA.
AC Q5L8U5;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE SubName: Full=Carbamoyl-phosphate synthase large chain 2 {ECO:0000313|EMBL:CAH09487.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:CAH09487.1};
GN Name=carB2 {ECO:0000313|EMBL:CAH09487.1};
GN Synonyms=pyrA2 {ECO:0000313|EMBL:CAH09487.1};
GN ORFNames=BF9343_3706 {ECO:0000313|EMBL:CAH09487.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09487.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH09487.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; CR626927; CAH09487.1; -; Genomic_DNA.
DR RefSeq; WP_005799108.1; NZ_UFTH01000001.1.
DR PaxDb; 272559-BF9343_3706; -.
DR GeneID; 66331354; -.
DR KEGG; bfs:BF9343_3706; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_3_10; -.
DR BioCyc; BFRA272559:G1GHZ-4057-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAH09487.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ SEQUENCE 1073 AA; 119474 MW; DE69E790F16D0878 CRC64;
MEKEMKKVLV LGSGALKIGQ AGEFDYSGSQ ALKALKEEGI NSVLVNPNIA TIQTSEGIAD
KVYFLPVTTY FVEEIIKKER PDGILLAFGG QTALNCGAEL YTKGILDKYG VKVLGTSVEA
IMYTEDRDLF VKKLDEIEMK TPISQAVESM EDAIAAARRI GYPVMVRSAY ALGGLGSGIC
ANEEEFLKLA ESSFAFSKQI LVEESLKGWK EIEFEVIRDA NDHCFTVASM ENFDPLGIHT
GESIVVAPTC SLDDKELKML QELSTKCIRH LGIVGECNIQ YAFNSDTDDY RVIEVNARLS
RSSALASKAT GYPLAFVAAK VALGYTLDQI GEMGTPNSAY VAPQLDYYIC KIPRWDLTKF
AGVSREIGSS MKSVGEIMSI GRSFEEIIQK GLRMIGQGMH GFVGNDDVHF EDLDKELSHP
TDLRIFALAQ AMEEGYTIER IHELTKIDPW FLGKLKNIVD YKAKLSAYDK VEDIPADVLR
EAKVLGFSDF QIARFVLNPV GNMEKENLMV RARRKELGIL PAVKRINTIA SEHPELTNYL
YMTYAVQGYD VNYYKNEKSV VVLGSGAYRI GSSVEFDWCS VNAVQTARKL GYKSIMINYN
PETVSTDYDM CDRLYFDELS FERVLDVIDL EQPRGVIVSV GGQIPNNLAM KLYRQSVPVL
GTSPISIDRA ENRNKFSAML DQLGIDQPAW QELTSLEDVK GFVEKVGYPV LVRPSYVLSG
AAMNVCYDDE ELENFLKMAA EVSKEYPVVV SQFLENTKEI EFDAVAQNGE VVEYAISEHI
EFAGVHSGDA TLVFPAQKIY FATARRIKKI SRQIAKELNI SGPFNIQFLA RNNEVKVIEC
NLRASRSFPF VSKVLKRNFI ETATRIMLDA PYSRPDKSAF DIDWIGVKAS QFSFSRLHKA
DPVLGVDMSS TGEVGCIGDD FSEALLNAMI ATGFKIPGKG VMFSSGAMKS KVDLLEASRM
LFNQGYKIYA TAGTAAFLNA HGVDTTPVYW PDEKPGAENN VMKMIADHKF DLIVNIPKNH
SKRELTNGYR IRRGAIDHNI PLITNARLAS AFIEAFCDLK LEDIQIKSWQ EYK
//
