ID A0A1W1Z137_9FIRM Unreviewed; 332 AA.
AC A0A1W1Z137;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00013007, ECO:0000256|HAMAP-Rule:MF_01109};
DE Short=OTCase {ECO:0000256|HAMAP-Rule:MF_01109};
DE EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007, ECO:0000256|HAMAP-Rule:MF_01109};
GN ORFNames=SAMN06297397_0825 {ECO:0000313|EMBL:SMC42103.1};
OS Clostridiales bacterium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1898207 {ECO:0000313|EMBL:SMC42103.1, ECO:0000313|Proteomes:UP000192328};
RN [1] {ECO:0000313|Proteomes:UP000192328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WTE2008 {ECO:0000313|Proteomes:UP000192328};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 -!- 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}.
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:SMC42103.1}.
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DR EMBL; FWXZ01000001; SMC42103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1Z137; -.
DR OrthoDB; 9802587at2; -.
DR Proteomes; UP000192328; Unassembled WGS sequence.
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:SF2; ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01109}.
FT DOMAIN 7..147
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 153..326
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 56..59
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 83
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 107
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 134..137
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 166
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 230
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 234..235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 271..272
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 316
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ SEQUENCE 332 AA; 36710 MW; 2380CF0DE8B15A85 CRC64;
MSSLKGKSFL KLLDFTPDEI SSLLDLAADL KAKKKAGIPH ACCAGKNVAL IFEKTSTRTR
CSFEVAAYDL GMNCTYLDPS GSQIGKKESI ADTARVLGRM YDGIEYRGFG QQIVEDLARY
SGVPVWNGLT NEYHPSQILA DFLTVRERFG SLKGIKLVYM GDARYNMGNS LMVGCAKMGM
HFVACAPEKY WPNSALIDTC RKIAAETGAV LEFEADVDKA VAGAHVIYTD VWVSMGEPDS
VWEERIHDLL PYRVTADVMR KAGSQCVFMH CLPSFHDLKT SIGRSIFEKF GIDCMEVTDE
VFESPASIVF DEAENRMHTI KAIMAATLSD KL
//
