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Database: UniProt
Entry: A0A1I0R150_9BACT
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ID   A0A1I0R150_9BACT        Unreviewed;       335 AA.
AC   A0A1I0R150;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=N-succinylornithine carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_02235};
DE            EC=2.1.3.11 {ECO:0000256|HAMAP-Rule:MF_02235};
DE   AltName: Full=N-succinyl-L-ornithine transcarbamylase {ECO:0000256|HAMAP-Rule:MF_02235};
DE            Short=SOTCase {ECO:0000256|HAMAP-Rule:MF_02235};
GN   Name=argF' {ECO:0000256|HAMAP-Rule:MF_02235};
GN   ORFNames=SAMN04488122_2024 {ECO:0000313|EMBL:SEW33869.1};
OS   Chitinophaga arvensicola.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=29529 {ECO:0000313|EMBL:SEW33869.1, ECO:0000313|Proteomes:UP000199310};
RN   [1] {ECO:0000313|EMBL:SEW33869.1, ECO:0000313|Proteomes:UP000199310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3695 {ECO:0000313|EMBL:SEW33869.1,
RC   ECO:0000313|Proteomes:UP000199310};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of the carbamoyl group from carbamoyl
CC       phosphate to the delta-amino group of N(2)-succinyl-L-ornithine to
CC       produce N(2)-succinyl-L-citrulline. Is essential for arginine
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + N(2)-succinyl-L-ornithine = H(+) + N(2)-
CC         succinyl-L-citrulline + phosphate; Xref=Rhea:RHEA:25884,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:58514, ChEBI:CHEBI:58862; EC=2.1.3.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02235};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02235}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_02235}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. SOTCase family. {ECO:0000256|HAMAP-Rule:MF_02235}.
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DR   EMBL; FOJG01000001; SEW33869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0R150; -.
DR   STRING; 29529.SAMN04488122_2024; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000199310; Unassembled WGS sequence.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   HAMAP; MF_02235; SOTCase; 1.
DR   InterPro; IPR043696; ArgF'-like.
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   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; PR00101; ATCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02235};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02235};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02235}.
FT   DOMAIN          21..179
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          204..330
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         66..69
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         94
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         129
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         161
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         166..169
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         196
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         257
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         293..294
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         297
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         321
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
SQ   SEQUENCE   335 AA;  37495 MW;  6DFD43AE067AF493 CRC64;
     MTGSVPLHLS TTCLKPIIEM KQFISTADVP SVPRLVDIAL NYKKDPFRDK ELGKNKTVGM
     IFLNPSLRTR LSTQVAAKNL GMEAIVFNID KEGWALEMND GAIMNGNTTE HVKEAAAVMG
     QYFDILAIRT FPGLKNKEED YTEKYINQFI KYAGVPVVSL ESATLHPLQS LTDVITIKEN
     WPHARKPKVV LTWAPHVKAL PQAVPNSFAQ WMNAWGETDF VITHPEGYEL DEKFSGNAHI
     EYDQDKALQD ADFVYVKNWS SYKDYGKITC TDPSWMFTNE KLALTNSAKV MHCLPVRRNV
     VIADEVLDGP NAIVIPEAGN RVWAAQAVLS EILKG
//
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