ID A0A0A1PHA3_RHIZD Unreviewed; 403 AA.
AC A0A0A1PHA3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN ORFNames=BCV71DRAFT_216557 {ECO:0000313|EMBL:ORE17480.1};
OS Rhizopus microsporus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE17480.1, ECO:0000313|Proteomes:UP000242381};
RN [1] {ECO:0000313|EMBL:ORE17480.1, ECO:0000313|Proteomes:UP000242381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE17480.1,
RC ECO:0000313|Proteomes:UP000242381};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; KV921354; ORE17480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1PHA3; -.
DR VEuPathDB; FungiDB:BCV72DRAFT_233569; -.
DR OMA; MRQTGFM; -.
DR Proteomes; UP000242381; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000242381}.
FT DOMAIN 48..329
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 403 AA; 44480 MW; F8BBD7BD6FA5AE13 CRC64;
MSPLSKFIVT PLASRRLFST TVAPHAYYTA SLVHDVSKKV NKNLKLYDFR SDTVTAPTDE
MFDLMKHASR SDDVFQEDKS VNDLQDYVAE LTGHEAALFC ASGTMTNQLA LRTHLVTPPH
SVVCDSRAHV FLWEAGGIAV HSRASVSPVI ASNGIHVTSE EIEANLLGED IYSAPTRVVS
LENTLNGMIF PIEELAKISK MARSKGLAMH LDGARLWNAS QETGISLKEY GKLFDSMSLC
LSKGVGAPIG SIVVGNAKFI DRVRHYRKLF GGGWRQAGFM AVAAKYGIEH IVPTMKETHQ
LAKYLADQLV AMGIDLQVPV HTNMVFIDTT RANIEIQRDL IPALAERNIK MGGMGKKARL
VLHHQIDRQG VDSFLEVMRD VVMAAHRNRK EEQSTRLALN NSA
//
