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Entry: A0A1M5UFL9_9BACT
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ID   A0A1M5UFL9_9BACT        Unreviewed;       319 AA.
AC   A0A1M5UFL9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN04488109_4660 {ECO:0000313|EMBL:SHH61832.1};
OS   Chryseolinea serpens.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Chryseolinea.
OX   NCBI_TaxID=947013 {ECO:0000313|EMBL:SHH61832.1, ECO:0000313|Proteomes:UP000184212};
RN   [1] {ECO:0000313|EMBL:SHH61832.1, ECO:0000313|Proteomes:UP000184212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24574 {ECO:0000313|EMBL:SHH61832.1,
RC   ECO:0000313|Proteomes:UP000184212};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQWQ01000003; SHH61832.1; -; Genomic_DNA.
DR   RefSeq; WP_073138785.1; NZ_FQWQ01000003.1.
DR   AlphaFoldDB; A0A1M5UFL9; -.
DR   STRING; 947013.SAMN04488109_4660; -.
DR   OrthoDB; 9802587at2; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000184212; 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   Reference proteome {ECO:0000313|Proteomes:UP000184212};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02235}.
FT   DOMAIN          2..160
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          186..312
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         47..50
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         75
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         110
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         142
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         147..150
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         178
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         239
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         275..276
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         279
FT                   /ligand="N(2)-succinyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:58514"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT   BINDING         303
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   319 AA;  35686 MW;  01446909BFB0A1C4 CRC64;
     MKNFISAADV PDIPGLVKKA LECKANPFKA KSLGAGKRMG LLFLNPSMRT RLSTQLAAQN
     LGMEAIVFNV GQDGWALEFE DEAIMSGNTV EHVKDAAPIL GNYFDVLGIR TFPSLQNKVD
     DYSELYINQF IKYAGIPVVS LESATLHPLQ SLTDVITIME NFDTTKRRPK IVLSWAPHVK
     ALPQCVANSF SQWINAWGQA DFVITHPEDY ELDERFTKGA TITTNQSEAL AQADFVYVKN
     WSTYTDYGRI YCNDPQWMLT NQKLALTNNA KVMHCLPVRR NVELSDEILD GPNSVVTQQA
     SNRVWAAQAV LSEILKEKH
//
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