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Database: UniProt
Entry: A0A2K8SYG3_9NOSO
LinkDB: A0A2K8SYG3_9NOSO
Original site: A0A2K8SYG3_9NOSO 
ID   A0A2K8SYG3_9NOSO        Unreviewed;       306 AA.
AC   A0A2K8SYG3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=COO91_06499 {ECO:0000313|EMBL:AUB40484.1};
OS   Nostoc flagelliforme CCNUN1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB40484.1, ECO:0000313|Proteomes:UP000232003};
RN   [1] {ECO:0000313|EMBL:AUB40484.1, ECO:0000313|Proteomes:UP000232003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB40484.1,
RC   ECO:0000313|Proteomes:UP000232003};
RA   Shang J.;
RT   "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT   its photosynthetic adaptation to extreme terrestrial habitat.";
RL   Submitted (NOV-2017) 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   -!- 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; CP024785; AUB40484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8SYG3; -.
DR   KEGG; nfl:COO91_06499; -.
DR   OrthoDB; 9802587at2; -.
DR   Proteomes; UP000232003; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232003};
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;  33426 MW;  057A1538111E539A CRC64;
     MAALLGRDLL SLADISPTEV QELLQLATQL KSQQLKLQCN KVLGLLFSKA STRTRVSFTV
     AMYQLGGQVI DLNPNVTQVS RGEPLQDTAR VLDRYLDILA IRTFAQQDLE TFAHYAKIPV
     INALTDAEHP CQVLADLLTI QESFNTLAGL TLTYVGDGNN MANSLMLGCA LVGMNVRIAT
     PSGYEPDSKI VEQARAIANN KTEVLVTDDP ELAAKDSAVL YTDVWASMGQ EAEADNRMPI
     FQPYQISEQL LSLAQPEAIV LHCLPAHRGE EITEAVIEGS QSRVWEQAEN RLHAQKALLA
     SILGAE
//
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