ID L1KYD4_9ACTN Unreviewed; 1102 AA.
AC L1KYD4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EKX65801.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EKX65801.1};
DE Flags: Fragment;
GN Name=carB {ECO:0000313|EMBL:EKX65801.1};
GN ORFNames=STRIP9103_01476 {ECO:0000313|EMBL:EKX65801.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX65801.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX65801.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX65801.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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:EKX65801.1}.
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DR EMBL; AEJC01000266; EKX65801.1; -; Genomic_DNA.
DR RefSeq; WP_009313758.1; NZ_AEJC01000266.1.
DR AlphaFoldDB; L1KYD4; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000010411; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01424; MGS_CPS_II; 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 HAMAP; MF_01210_B; CPSase_L_chain_B; 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; IPR033937; MGS_CPS_CarB.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EKX65801.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000010411};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..334
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 682..873
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 955..1100
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1102
FT /evidence="ECO:0000313|EMBL:EKX65801.1"
SQ SEQUENCE 1102 AA; 117890 MW; 45DE6E709C7051BE CRC64;
MPKRTDIQSV LVIGSGPIVI GQAAEFDYSG TQACRVLKAE GLRVILVNSN PATIMTDPEI
ADATYVEPIT PEFVEKIIAK ERPDALLPTL GGQTALNTAI SLHENGVLEK YGVELIGANV
EAIHKGEDRD QFKLVVDAVN AKIGHGESAR SVICHSMEDV LAGVETLGGY PVVVRPSFTM
GGAGSGFAHD EEELRRIAGT GLTLSPTTEV LLEESILGWK EYELELMRDK HDNVVVVCSI
ENFDPMGVHT GDSITVAPAM TLTDREYQIL RDIGIAVIRE VGVDTGGCNI QFAVNPEDGR
VIVIEMNPRV SRSSALASKA TGFPIAKIAA KLAVGYTLDE IPNDITQETP ASFEPTLDYV
VVKAPRFAFE KFPSADSSLT TTMKSVGEAM AIGRNFTEAL QKALRSLEKK GSQFTFVGEP
GDKTELLREA VRPTDGRINT VMQAIRAGAT PEEVFEATKI DPWFVDQLFL IKEIADELAA
AERLDAELLA EAKRHGFSDQ QIGEIRGLRE DVVREVRHAL GVRPVYKTVD TCAAEFAAKT
PYFYSSYDEE TEVAPREKPA VIILGSGPNR IGQGIEFDYS CVHASFALSD AGYETVMVNC
NPETVSTDYD TSDRLYFEPL TLEDVLEIVH AESLAGPIAG VVVQLGGQTP LGLSQALKDN
GVPIVGTSPE AIHAAEDRGA FGRVLAEAGL PAPKHGTATT FAGAKAIADE IGYPVLVRPS
YVLGGRGMEI VYDETRLESY IAESTEISPS RPVLVDRFLD DAIEIDVDAL YDGEELYLGG
VMEHIEEAGI HSGDSACALP PITLGGFDIK RLRASTEAIA RGVGVRGLIN IQFAMAGDIL
YVLEANPRAS RTVPFTSKAT AVPLAKAAAR ISLGATIAEL RAEGLLPAVG DGGELPLDAP
ISVKEAVMPW SRFRDIHGRG VDTVLGPEMR STGEVMGIDS VFGTAYAKSQ AGAYGPLPTK
GRAFISVANR DKRSMIFPAR ELVAHGFELL ATSGTAEVLK RNGIHATVVR KHSEGTGPNG
ERTIVQLIHD GEVDLIVNTP YGTGGRLDGY DIRTAAVARS VPCLTTVQAL AAAVQGIDAL
NHGDVGVRSL QEHAEHLTAA RD
//
