ID C9LRV9_SELS3 Unreviewed; 310 AA.
AC C9LRV9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00013007};
DE EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007};
GN Name=argF {ECO:0000313|EMBL:EEX78377.1};
GN OrderedLocusNames=Selsp_1033 {ECO:0000313|EMBL:AEB99992.1};
GN ORFNames=SELSPUOL_00179 {ECO:0000313|EMBL:EEX78377.1};
OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX78377.1, ECO:0000313|Proteomes:UP000003505};
RN [1] {ECO:0000313|EMBL:EEX78377.1, ECO:0000313|Proteomes:UP000003505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:EEX78377.1}, and ATCC 35185 / DSM
RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000003505};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEB99992.1, ECO:0000313|Proteomes:UP000011124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:AEB99992.1}, and ATCC 35185 / DSM
RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000011124};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Selenomonas sputigena DSM 20758.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001065, ECO:0000256|HAMAP-
CC Rule:MF_01109};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004975}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805,
CC ECO:0000256|HAMAP-Rule:MF_01109}.
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DR EMBL; CP002637; AEB99992.1; -; Genomic_DNA.
DR EMBL; ACKP02000003; EEX78377.1; -; Genomic_DNA.
DR RefSeq; WP_006190806.1; NZ_GG698596.1.
DR AlphaFoldDB; C9LRV9; -.
DR STRING; 546271.Selsp_1033; -.
DR KEGG; ssg:Selsp_1033; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_2_9; -.
DR OrthoDB; 9802587at2; -.
DR Proteomes; UP000003505; Unassembled WGS sequence.
DR Proteomes; UP000011124; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR HAMAP; MF_01109; OTCase; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR002292; Orn/put_carbamltrans.
DR InterPro; IPR024904; OTCase_ArgI.
DR NCBIfam; TIGR00658; orni_carb_tr; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109};
KW Reference proteome {ECO:0000313|Proteomes:UP000011124};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01109}.
FT DOMAIN 5..145
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 152..307
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 54..57
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 81
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 105
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 132..135
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 164
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 228
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 232..233
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 268..269
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 296
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ SEQUENCE 310 AA; 34200 MW; DAADDDFBEFDDCBB5 CRC64;
MLKGRDLLSI HDLSVEEVEA ILALAEELKA MQKAGIEHRV LAGKTLGMIF EKSSTRTRVS
FETGMFQLGG QALFLSNRDL QIGRGEPIKD TARVLSRYLD GVMIRTFEHE KVEEFAKYAD
IPVINALTDL LHPCQALTDL LTIREHKGKN LKGLKMAYVG DGNNMTHSLM YAAAKTGMNF
VAATPADYAP DEGVTQRAQE DAKETGASIT LVTDPFAAAK DADILVTDTW ASMGQEAEHE
ERKKIFAPYQ INGDLLAAAD KRAIVMHCLP AYRGEEITED VMEAFSDVIF DEAENRLHTQ
KAILALLMAD
//
