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
//