ID   OTC_HAEIG               Reviewed;         334 AA.
AC   A5UHA3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Ornithine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01109};
DE            Short=OTCase {ECO:0000255|HAMAP-Rule:MF_01109};
DE            EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN   Name=arcB {ECO:0000255|HAMAP-Rule:MF_01109};
GN   OrderedLocusNames=CGSHiGG_06290;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC       carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC       produce L-citrulline. {ECO:0000250}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01109};
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01109}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000255|HAMAP-Rule:MF_01109}.
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DR   EMBL; CP000672; ABR00159.1; -; Genomic_DNA.
DR   RefSeq; WP_012055120.1; NC_009567.1.
DR   AlphaFoldDB; A5UHA3; -.
DR   SMR; A5UHA3; -.
DR   EnsemblBacteria; ABR00159; ABR00159; CGSHiGG_06290.
DR   KEGG; hiq:CGSHiGG_06290; -.
DR   HOGENOM; CLU_043846_3_1_6; -.
DR   OMA; VYVKNWS; -.
DR   UniPathway; UPA00254; UER00365.
DR   Proteomes; UP000001990; 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   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019546; P:arginine deiminase pathway; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1370; -; 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   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Cytoplasm; Transferase.
FT   CHAIN           1..334
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_1000065094"
FT   BINDING         57..60
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         84
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         108
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         135..138
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         168
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         232
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         236..237
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         274..275
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         321
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   334 AA;  37620 MW;  49DD38C982C2FDDE CRC64;
     MAFNMKNRHL LSLVHHTERE IKYLLDLSRD LKRAKYAGTE QQKLKGKNIA LIFEKTSTRT
     RCAFEVAAYD QGAQVTYIDP NSSQIGHKES MKDTARVLGR MYDGIEYRGF KQSIVQELAD
     YAGVPVFNGL TDEFHPTQML ADVLTMIEHC DKPLSEISYV YIGDARNNMG NSLLLIGAKL
     GMDVRICAPK ALLPEASLVE MCEKFAKESG ARITVTEDID KAVKGVDFVH TDVWVSMGEP
     LETWGERIKL LLPYQVTPEL MKRTGNPKVK FMHCLPAFHN SETKVGRQIA EKYPELANGI
     EVTEEVFESP MNIAFEQAEN RMHTIKAVMV ASLA