ID A0A0F6TSF0_9GAMM Unreviewed; 333 AA.
AC A0A0F6TSF0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=TQ33_1837 {ECO:0000313|EMBL:AKE52775.1};
OS Kangiella geojedonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE52775.1, ECO:0000313|Proteomes:UP000034071};
RN [1] {ECO:0000313|EMBL:AKE52775.1, ECO:0000313|Proteomes:UP000034071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCS-5 {ECO:0000313|EMBL:AKE52775.1,
RC ECO:0000313|Proteomes:UP000034071};
RA Kim K.M.;
RT "Complete genome sequence of Kangiella geojedonensis strain YCS-5T.";
RL Submitted (FEB-2015) 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}.
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DR EMBL; CP010975; AKE52775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F6TSF0; -.
DR STRING; 914150.TQ33_1837; -.
DR KEGG; kge:TQ33_1837; -.
DR PATRIC; fig|914150.5.peg.1863; -.
DR HOGENOM; CLU_043846_3_3_6; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000034071; Chromosome.
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:UP000034071};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02234}.
FT DOMAIN 2..159
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 181..328
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_02234"
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_02234"
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_02234"
FT BINDING 142
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 146..149
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 248
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 290..291
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 291
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 318
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 90
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 298
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
SQ SEQUENCE 333 AA; 38008 MW; B31005CE79114DDE CRC64;
MKHFLTTEHW SQNDLQQMID FAKELKEEKF QPLLKNKSVA LLFFNPSLRT RTSFELGVHQ
LGGQAIVLQP GKDAWPIEFE LGSIMDGEAE EHIQEVAQVL SAYCDIIAVR AFPKFQNWQD
DRQDKLIKSL AQFSTVPVIN METITHPCQE LAHIMALQEN LGDLKGKKYV LTWTYHPKPL
NTAVANSSLM IASKFGMDVT LLCPNEDYLL DQHYMDLGQT YSSQHGNQLT VSHDIDSAYE
GADVVYAKSW GALPYFGQWE KEKPMRDQYK HFMVDEAKMA KTNNALFSHC LPMRRNVKAT
DGVVDSKNCI AIQEAENRLH VQKSMMNTLI NHS
//
