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Database: UniProt
Entry: I7HE27_9HELI
LinkDB: I7HE27_9HELI
Original site: I7HE27_9HELI 
ID   I7HE27_9HELI            Unreviewed;       328 AA.
AC   I7HE27;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   Name=argF {ECO:0000313|EMBL:BAM31404.1};
GN   ORFNames=HCBAA847_0149 {ECO:0000313|EMBL:BAM31404.1}, HCCG_02042
GN   {ECO:0000313|EMBL:EFR47494.1};
OS   Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM31404.1, ECO:0000313|Proteomes:UP000006036};
RN   [1] {ECO:0000313|EMBL:EFR47494.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 18818 {ECO:0000313|EMBL:EFR47494.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA   Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA   Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Helicobacter cinaedi strain CCUG 18818.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAM31404.1, ECO:0000313|Proteomes:UP000006036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31404.1,
RC   ECO:0000313|Proteomes:UP000006036};
RX   PubMed=23012276; DOI=10.1128/JB.01347-12;
RA   Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT   "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT   BAA-847.";
RL   J. Bacteriol. 194:5692-5692(2012).
RN   [3] {ECO:0000313|EMBL:BAM31404.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31404.1};
RA   Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000005755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 18818 {ECO:0000313|Proteomes:UP000005755};
RX   PubMed=25212613;
RA   Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA   Fox J.G.;
RT   "Draft genome sequences of six enterohepatic helicobacter species isolated
RT   from humans and one from rhesus macaques.";
RL   Genome Announc. 2:e00857-e00814(2014).
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; AP012492; BAM31404.1; -; Genomic_DNA.
DR   EMBL; DS990393; EFR47494.1; -; Genomic_DNA.
DR   RefSeq; WP_002957382.1; NZ_DS990393.1.
DR   AlphaFoldDB; I7HE27; -.
DR   KEGG; hcb:HCBAA847_0149; -.
DR   PATRIC; fig|1206745.3.peg.158; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_2_7; -.
DR   OrthoDB; 9802587at2; -.
DR   Proteomes; UP000005755; Unassembled WGS sequence.
DR   Proteomes; UP000006036; Chromosome 1.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01109}.
FT   DOMAIN          2..142
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          161..311
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         51..54
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         78
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         102
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         129..132
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         169
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         233
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         237..238
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         273..274
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         301
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   328 AA;  36707 MW;  FAD3E84C88E33574 CRC64;
     MRHFLTLNDF SKDEILAVTN LALKLKQELR NSNHTPYLKG KILAMIFEKS STRTRVSFEG
     GIYQLGGHGM FLSHKDIQLG RGEPIKDTSR VISSMVDMVM MRTDRHEKLQ EFAEYSSVPI
     INGLSDDFHP VQLMADYLTM LECGIALPDG IHKNGLKKPI VAYIGDGNNM AHSWINLAAI
     LGFELRVASP LGYFPRTDII ESALKTCKQS GGAIHIMQEP QKAVSGVNVV VTDTWASMGQ
     EEQKKEREKA FVGFCVDDSL MNLAQEDAIF LHCLPAYRGQ EVSESVLEGK QSRVFQEANN
     RLHAQKAIML ALVRLNNLPL AYPLEMEL
//
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