ID F5XQF6_MICPN Unreviewed; 325 AA.
AC F5XQF6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Threo-3-hydroxyaspartate ammonia-lyase {ECO:0000313|EMBL:BAK34456.1};
DE EC=4.3.1.16 {ECO:0000313|EMBL:BAK34456.1};
GN OrderedLocusNames=MLP_14420 {ECO:0000313|EMBL:BAK34456.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK34456.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK34456.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; AP012204; BAK34456.1; -; Genomic_DNA.
DR AlphaFoldDB; F5XQF6; -.
DR STRING; 1032480.MLP_14420; -.
DR KEGG; mph:MLP_14420; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_11; -.
DR Proteomes; UP000007947; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0030848; F:threo-3-hydroxyaspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR43050; SERINE / THREONINE RACEMASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43050:SF1; SERINE RACEMASE; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:BAK34456.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000007947}.
FT DOMAIN 28..312
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 325 AA; 33932 MW; 4F6009C847D27E98 CRC64;
MSALDTAPRL PTYADVEAAA RRIAGVAHRT PVMTSRTANE RTGAELFFKC ENLQRSGAFK
FRGALNAIRS LPAEQRERGV VAFSSGNHAQ AIAYAGQLEG VRTVIVMPTD APTLKLAATK
GYGGEIVRYD RYRQDREEIG RQLAVEQGLA LIPPFNHPDV IAGQGTAAKE LFEETGPLDA
LLVCTGGGGL TSGCALAAQA LSPGCQVIGV EPQAGDDIQQ SLAAGRIVTI PVPRSIADGA
LTTAPGSLTF ALLQQLGVRV VTVPDEALIE TMRFFVERMK LVVEPTGCLA AAAAFSGAVP
VESKHVGVII SGGNVDPAAL AGYLT
//
