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Database: UniProt
Entry: A0A0M4T267_9NOSO
LinkDB: A0A0M4T267_9NOSO
Original site: A0A0M4T267_9NOSO 
ID   A0A0M4T267_9NOSO        Unreviewed;       306 AA.
AC   A0A0M4T267;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=ACX27_12475 {ECO:0000313|EMBL:ALF53470.1};
OS   Nostoc piscinale CENA21.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=224013 {ECO:0000313|EMBL:ALF53470.1, ECO:0000313|Proteomes:UP000062645};
RN   [1] {ECO:0000313|Proteomes:UP000062645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA21 {ECO:0000313|Proteomes:UP000062645};
RA   Leao T.F., Leao P.N., Guimaraes P.I., de Melo A.G.C., Ramos R.T.J.,
RA   Silva A., Fiore M.F., Schneider M.P.C.;
RT   "Genome Of Nitrogen-Fixing Cyanobacterium Nostoc piscinale CENA21 From
RT   Solimoes/Amazon River Floodplain Sediments And Comparative Genomics To
RT   Uncover Biosynthetic Natural Products Potential.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALF53470.1, ECO:0000313|Proteomes:UP000062645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA21 {ECO:0000313|EMBL:ALF53470.1,
RC   ECO:0000313|Proteomes:UP000062645};
RX   PubMed=27034496;
RA   Leao T., Guimaraes P.I., de Melo A.G., Ramos R.T., Leao P.N., Silva A.,
RA   Fiore M.F., Schneider M.P.;
RT   "Draft Genome Sequence of the N2-Fixing Cyanobacterium Nostoc piscinale
RT   CENA21, Isolated from the Brazilian Amazon Floodplain.";
RL   Genome Announc. 4:0-0(2016).
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; CP012036; ALF53470.1; -; Genomic_DNA.
DR   RefSeq; WP_062292719.1; NZ_CP012036.1.
DR   AlphaFoldDB; A0A0M4T267; -.
DR   STRING; 224013.ACX27_12475; -.
DR   PATRIC; fig|224013.5.peg.3019; -.
DR   OrthoDB; 9802587at2; -.
DR   Proteomes; UP000062645; 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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01109}.
FT   DOMAIN          7..142
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          149..301
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         160
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         223
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         227..228
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   306 AA;  33471 MW;  2023C688F3EC4383 CRC64;
     MAVLIGRDIL SLADFSPTEL QEILQLAGQL KSQQLKLRCN KVLGLLFSKA STRTRVSFTV
     AMYQLGGQVI DLHPNVTQVS RGEPIQDTAR VLDRYLDVLA IRTFAQEDLE IFANYAKIPV
     INALTDAEHP CQILADLLTI QECFGKLAGL TLTYVGDGNN VANSLMLGCA LAGMNVRVAT
     PKGFEPDAKI VEQARAIAAG KTEVLLTHDP ELAAKDASVL YTDVWASMGQ EQEADDRMPI
     FQPYQISEQL LSLADQDAIV LHCLPAHRGE EITEEVIEGS HSRVWDQAEN RLHAQKALLA
     SILGAE
//
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