ID F3PI82_9BACE Unreviewed; 317 AA.
AC F3PI82;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=HMPREF9445_01722 {ECO:0000313|EMBL:EGF51784.1};
OS Bacteroides clarus YIT 12056.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF51784.1, ECO:0000313|Proteomes:UP000010321};
RN [1] {ECO:0000313|EMBL:EGF51784.1, ECO:0000313|Proteomes:UP000010321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF51784.1,
RC ECO:0000313|Proteomes:UP000010321};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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:EGF51784.1}.
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DR EMBL; AFBM01000018; EGF51784.1; -; Genomic_DNA.
DR RefSeq; WP_005656370.1; NZ_GL882592.1.
DR AlphaFoldDB; F3PI82; -.
DR STRING; 762984.SAMN05444376_2760; -.
DR GeneID; 31797945; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_3_10; -.
DR OrthoDB; 9802587at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000010321; 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 3..160
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 183..306
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 236
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT BINDING 274..275
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 278
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02235"
FT BINDING 302
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 317 AA; 36339 MW; AD1EDB35CE087382 CRC64;
MKNFTCVQDI GNLKTALDEA FEIKKDRFKY VELGRNKTLM MIFFNSSLRT RLSTQKAALN
LGMNVIVLDI NQGAWKLETE RGVIMDGDKP EHLLEAIPVM GCYCDVIGVR SFARFEDREY
DYNEVILNQF IKYSGRPVFS MEAATRHPLQ SFADLITIEE YKKTARPKVV MTWAPHPRPL
PQAVPNSFAE WMNATDYDFV ITHPEGYELD PKFVGNARVE YDQMKAFEGA DFVYAKNWAA
YTGDNYGQIL SKDRDWTVSD RQMAVTNNAY FMHCLPVRRN MIVTDDVIES PQSIVIPEAA
NREISATVVL KRLIEGL
//
