ID D7ATA1_THEM3 Unreviewed; 313 AA.
AC D7ATA1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00013007};
DE EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007};
GN OrderedLocusNames=Tmath_0595 {ECO:0000313|EMBL:ADH60348.1};
OS Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG
OS 53645 / CIP 108742 / A3).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH60348.1, ECO:0000313|Proteomes:UP000002064};
RN [1] {ECO:0000313|EMBL:ADH60348.1, ECO:0000313|Proteomes:UP000002064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11426 / CIP 108742 / A3
RC {ECO:0000313|Proteomes:UP000002064};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT mathranii str. A3.";
RL Submitted (MAY-2010) 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}.
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DR EMBL; CP002032; ADH60348.1; -; Genomic_DNA.
DR RefSeq; WP_012994657.1; NC_014209.1.
DR AlphaFoldDB; D7ATA1; -.
DR STRING; 583358.Tmath_0595; -.
DR KEGG; tmt:Tmath_0595; -.
DR HOGENOM; CLU_043846_3_2_9; -.
DR Proteomes; UP000002064; 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: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 8..148
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 155..310
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 167
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 231
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 235..236
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 272..273
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 300
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ SEQUENCE 313 AA; 35079 MW; DECDD1D577D776F9 CRC64;
MAFNLKGRSL LTLKDYTPQE IRYILDIAKQ VKAERKAGVV HQRFLGKTIA LIFEKRSTRT
RCAFETAFGE EGGHPVFLST DDIQLGAKES IEDTARVLGR MFDAIEFRGF KQETVEILAK
YAGVPVYNGL TDEYHPTQVL ADLMTIEEEF GSLTGRKLVF VGDGRNNMAN TLAVGCAKMG
MHYVINSPKE LWPSQEFIDE IRQMAAENGG TFELTSVPGE GLEGADAIYT DVWASMGEEA
KAEEREALLR PFQVNEEMMK KTGREDTIFL HCLPAVKGQE VTFDVIEGKQ SRVWDQAENR
KHTIKAVMIA TLL
//
