ID Q0AMP2_MARMM Unreviewed; 338 AA.
AC Q0AMP2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE SubName: Full=L-threonine aldolase {ECO:0000313|EMBL:ABI66445.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:ABI66445.1};
GN OrderedLocusNames=Mmar10_2153 {ECO:0000313|EMBL:ABI66445.1};
OS Maricaulis maris (strain MCS10).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI66445.1, ECO:0000313|Proteomes:UP000001964};
RN [1] {ECO:0000313|EMBL:ABI66445.1, ECO:0000313|Proteomes:UP000001964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI66445.1,
RC ECO:0000313|Proteomes:UP000001964};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; CP000449; ABI66445.1; -; Genomic_DNA.
DR RefSeq; WP_011644090.1; NC_008347.1.
DR AlphaFoldDB; Q0AMP2; -.
DR STRING; 394221.Mmar10_2153; -.
DR KEGG; mmr:Mmar10_2153; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_049619_0_0_5; -.
DR OMA; ETDCEVF; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000001964; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ABI66445.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001964}.
FT DOMAIN 2..297
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 338 AA; 36309 MW; 3A157A187A0FFFBA CRC64;
MNFLSDTTAP AHPDLIEAIA AANRDFAPSY GADPVSARVE AQLKAIFETD LKVLFAVSGT
ASNALALSVL CPSHGAILCH DEAHIHRDER GAPEFFTGGG KLIPLPGDHA KIGMDGLERA
LAEIPEGFVH TSPVRVLSLS NLSESGTAYT PSEVRERAGR VKDRPALVHM DGARFANALV
TLGCSPAELT WKAGVNALCF GATKNGALGA EAVILFPSVM DRFEELQARQ KRAGHMAPKM
RFMAAQFEAW LRDDLWLDLA RTANARAKTL ADGFRCVDGA EVLHPVDGNE IFVRLDEAIA
AKMRDAGAQF YQWPDGSARF VTSWCTTKAE IVATLAAI
//