ID A0A086ADT5_9FLAO Unreviewed; 319 AA.
AC A0A086ADT5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=IW15_05290 {ECO:0000313|EMBL:KFF14849.1};
OS Chryseobacterium soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF14849.1, ECO:0000313|Proteomes:UP000028705};
RN [1] {ECO:0000313|EMBL:KFF14849.1, ECO:0000313|Proteomes:UP000028705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF14849.1,
RC ECO:0000313|Proteomes:UP000028705};
RA Stropko S.J., Pipes S.E., Newman J.;
RT "Genome of Chryseobacterium soli DSM 19298.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFF14849.1}.
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DR EMBL; JPRH01000001; KFF14849.1; -; Genomic_DNA.
DR RefSeq; WP_034709733.1; NZ_JPRH01000001.1.
DR AlphaFoldDB; A0A086ADT5; -.
DR STRING; 445961.IW15_05290; -.
DR eggNOG; COG0078; Bacteria.
DR OrthoDB; 9802587at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000028705; 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 2..160
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 184..310
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 177
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 273..274
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 277
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT BINDING 301
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; 36084 MW; FB57E51BCC5D8C30 CRC64;
MKNFTSVSDI ENLQDIIKKA LQIKENPLSD TEKGKGKTIG LVFLNSSLRT RLSSQIAAQN
LGLNVLTLNA AQEAWNLEFA DGAVMNGDTV EHIKDAIEVL NQYCDIIAVR CFAGMKSKED
DVNESIMSQF EKHAKVPVVS LESATRHPLQ SLADCITITE NWKEERKPKV VLTWAPHIKP
IAQAVGNSFT EWMQEMDVDF VIANPEGYDL DKNFTKDTKV FHNQDEALKD ADFVYVKNWS
SFDEYATMPE VKESWMLTAE KLENTNNAKV MHCLPVRRNV ELSDEVMDGE NSIIYQQAKN
RIFSAQAVFS EILDELKSK
//
