ID A0A411EBY1_9FLAO Unreviewed; 313 AA.
AC A0A411EBY1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=EQY75_11220 {ECO:0000313|EMBL:QBA65044.1};
OS Muriicola soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Muriicola.
OX NCBI_TaxID=2507538 {ECO:0000313|EMBL:QBA65044.1, ECO:0000313|Proteomes:UP000290889};
RN [1] {ECO:0000313|EMBL:QBA65044.1, ECO:0000313|Proteomes:UP000290889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY002 {ECO:0000313|EMBL:QBA65044.1,
RC ECO:0000313|Proteomes:UP000290889};
RA Kang H.J., Kim S.B.;
RT "Muriicola soli sp. nov., isolated from soil.";
RL Submitted (JAN-2019) 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; CP035544; QBA65044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411EBY1; -.
DR KEGG; mur:EQY75_11220; -.
DR OrthoDB; 9802587at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000290889; Chromosome.
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:UP000290889};
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 183..307
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 176
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT BINDING 237
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT BINDING 270..271
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 274
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT BINDING 298
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 313 AA; 35207 MW; 4F80A72CB33AEB2B CRC64;
MKHYLSIDDI DSIPSWLSLA AECKKAPLKY RKLGEGKVLG LLFFNNSLRT RLSTQKAAFH
LGMHCMTMNF GSEGWALEFE DGTIMDQGKA EHIKEAAQVV SQYCDVLGVR AFASLTDKEK
DEAEMVLNGF KKYASIPILN MESATGHPLQ AFADLITISE HSQKKNPKIV LSWAPHPKAL
PHAVANSFIK MMGQNPQFEF SITHPMGYEL NQDLVQHIPV SYDQNKALKD ADFVYVKNWS
AYQPYGAVLN NDPHWMLTQD KLGQAKFMHC LPVRRNVVVE DRVLDGNNSL VIQQANNRTY
AAQVALLKIL ESL
//
