ID A0A0A2WE76_9GAMM Unreviewed; 342 AA.
AC A0A0A2WE76;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=N-acetylornithine carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_02234};
DE EC=2.1.3.9 {ECO:0000256|HAMAP-Rule:MF_02234};
DE AltName: Full=N-acetyl-L-ornithine transcarbamylase {ECO:0000256|HAMAP-Rule:MF_02234};
DE Short=AOTCase {ECO:0000256|HAMAP-Rule:MF_02234};
DE Short=Acetylornithine transcarbamylase {ECO:0000256|HAMAP-Rule:MF_02234};
GN Name=argF' {ECO:0000256|HAMAP-Rule:MF_02234};
GN ORFNames=LF41_536 {ECO:0000313|EMBL:KGQ18511.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ18511.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ18511.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ18511.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-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)-acetyl-L-ornithine to
CC produce N(2)-acetyl-L-citrulline. This is a step in an alternative
CC arginine biosynthesis pathway. {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + N(2)-acetyl-L-ornithine = H(+) + N(2)-
CC acetyl-L-citrulline + phosphate; Xref=Rhea:RHEA:18609,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57805,
CC ChEBI:CHEBI:58228, ChEBI:CHEBI:58765; EC=2.1.3.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02234};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. AOTCase family. {ECO:0000256|HAMAP-Rule:MF_02234}.
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:KGQ18511.1}.
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DR EMBL; JRKJ01000018; KGQ18511.1; -; Genomic_DNA.
DR RefSeq; WP_036169776.1; NZ_JRKJ01000018.1.
DR AlphaFoldDB; A0A0A2WE76; -.
DR STRING; 1300345.LF41_536; -.
DR PATRIC; fig|1300345.3.peg.2207; -.
DR eggNOG; COG0078; Bacteria.
DR OrthoDB; 9802587at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000030518; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0043857; F:N-acetylornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR HAMAP; MF_02234; AOTCase; 1.
DR InterPro; IPR043695; ArgF.
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_02234};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02234};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02234};
KW Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02234}.
FT DOMAIN 7..165
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 190..336
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 53..56
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_02234"
FT BINDING 81
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_02234"
FT BINDING 116
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_02234"
FT BINDING 148
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 152..155
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_02234"
FT BINDING 256
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 298..299
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_02234"
FT BINDING 299
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 326
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_02234"
FT SITE 96
FT /note="Key residue in conferring substrate specificity for
FT N-acetyl-L-ornithine versus N-succinyl-L-ornithine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT MOD_RES 306
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
SQ SEQUENCE 342 AA; 38309 MW; 9B1F322CE6C1C35C CRC64;
MKQVPLRHFL NTQDWSRDEL DAVLAMAAQY KQQPLGPRAL EGKSIALVFF NSSMRTRTSF
EIGAFQLGGH AVVLQPGKDA WPIEFDLGTV MDGETEEHIA EVARVLSRYV DLIGVRAFPK
FVDWSLDRED RVLKGFAKYS SVPVINMETI THPCQELAHI LALQEHFGTT DLRGKKYVLT
WTYHPKPLNT AVANSALTIA TRMGMDVTLL CPTPEYILDE RYMQWAAQNV AESGGSLQVS
HDIESAYRGA DAVYAKSWGA LPYFGNWAPE KPIRDAHQHF IVDEAKMALT NNGVFSHCLP
LRRNVKATDA VMDSPQCIAI DEAENRLHVQ KAVMASLIGQ RR
//
