ID C6ABC4_BARGA Unreviewed; 311 AA.
AC C6ABC4;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-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:ACS50491.1};
GN OrderedLocusNames=Bgr_01070 {ECO:0000313|EMBL:ACS50491.1};
OS Bartonella grahamii (strain as4aup).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS50491.1, ECO:0000313|Proteomes:UP000001489};
RN [1] {ECO:0000313|EMBL:ACS50491.1, ECO:0000313|Proteomes:UP000001489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F.,
RA Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H., Andersson S.G.;
RT "Run-off replication of host-adaptability genes is associated with gene
RT transfer agents in the genome of mouse-infecting Bartonella grahamii.";
RL PLoS Genet. 5:E1000546-E1000546(2009).
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:0000256|ARBA:ARBA00003822}.
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; CP001562; ACS50491.1; -; Genomic_DNA.
DR RefSeq; WP_012754529.1; NC_012846.1.
DR AlphaFoldDB; C6ABC4; -.
DR STRING; 634504.Bgr_01070; -.
DR KEGG; bgr:Bgr_01070; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_2_5; -.
DR OrthoDB; 9802587at2; -.
DR Proteomes; UP000001489; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01109}.
FT DOMAIN 6..146
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 153..302
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 55..58
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 82
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 106
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 133..136
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 224
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 228..229
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 263..264
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT BINDING 291
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ SEQUENCE 311 AA; 34819 MW; BD517452B321EDF4 CRC64;
MTNALRHFTD LSILTPAIAR ALIDYAKILK ASFKAGKGSK PFIGKTLAMI FEKPSTRTRI
SFDISMRQLG GDTIMLTGSE MQLGHSETIA DTARVLSRFV DIVILRTTKH QRMLELAQYA
QIPVINALTD DTHPCQILAD ILTYEEHRGP IAGKIFAWMG DGNNVLHSLI EAAALFDFHL
RIATPKGSEP QEKFIHWARE RGAHLTLTHS PQKAAQDADC IMTDTWVSMG QEFRARSHSI
FLPYQVNEAL MKLAKSDALF MHCLPAHRGE EVVDSIIDGL HSVVFDEAEN RLHVQKAILS
WCLQDAFFSP Q
//
