ID V2QIM2_9BACT Unreviewed; 386 AA.
AC V2QIM2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:USF23911.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:USF23911.1};
GN Name=argD {ECO:0000313|EMBL:USF23911.1};
GN ORFNames=N508_000984 {ECO:0000313|EMBL:USF23911.1}, N508_00445
GN {ECO:0000313|EMBL:ESJ99144.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ99144.1};
RN [1] {ECO:0000313|EMBL:ESJ99144.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ99144.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF23911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23911.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF23911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23911.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; AYGZ01000009; ESJ99144.1; -; Genomic_DNA.
DR EMBL; CP097562; USF23911.1; -; Genomic_DNA.
DR RefSeq; WP_023275281.1; NZ_FTRD01000023.1.
DR AlphaFoldDB; V2QIM2; -.
DR STRING; 1379858.N508_00445; -.
DR GeneID; 78587719; -.
DR PATRIC; fig|1379858.3.peg.438; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_0; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000017429; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000313|EMBL:USF23911.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000017429};
KW Transferase {ECO:0000313|EMBL:USF23911.1}.
SQ SEQUENCE 386 AA; 41848 MW; BEBDF2ECDDD6E241 CRC64;
MSSLMNNYGR FKISFAYGLG AKLYTADNEE YLDFASGISV TNLGHNFKPL TDAVCSQAAK
VMHTSNLYEI PLQEELADLI SKNSFNGKVF FCNSGAEANE AAIKLARLYG NTIHHGKKYK
IISMYNSFHG RTYATMGATA QEKIQKGSYP MPGYNQYIPF NNIEAFKNAV SLNDTAAIIL
ELFQGEGGVI PVDIEFLKEV RRICDEKDIL MIVDEVQTGY GRTGELFAYK LFGVVPDIMT
LSKSIAGGVP MGAVVSVEKA ASLFTGGTHG STFGGNPLAC AAGIAVIKEM TKEGFLQSVK
EKGALLKDYL YKNLSDTCLV KGEGLLIGVK TPYSPKDVAE ACLENHLLVV TAGNNSVRLY
PPLNISSEDL LKGAEIFVST IKELGK
//
