ID Q07ZC3_SHEFN Unreviewed; 336 AA.
AC Q07ZC3;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=L-threonine aldolase {ECO:0000313|EMBL:ABI72641.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:ABI72641.1};
GN OrderedLocusNames=Sfri_2801 {ECO:0000313|EMBL:ABI72641.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI72641.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI72641.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI72641.1,
RC ECO:0000313|Proteomes:UP000000684};
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 Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
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; CP000447; ABI72641.1; -; Genomic_DNA.
DR RefSeq; WP_011638250.1; NC_008345.1.
DR AlphaFoldDB; Q07ZC3; -.
DR STRING; 318167.Sfri_2801; -.
DR KEGG; sfr:Sfri_2801; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_3_6; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000000684; 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; 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 Lyase {ECO:0000313|EMBL:ABI72641.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000684}.
FT DOMAIN 3..284
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 336 AA; 36112 MW; 6DF69D77C0C3CC1D CRC64;
MIDFRSDTVT QPTEAMRLAM SRAEVGDDVY GDDPTVNNLQ DMAAEMFGFD GALFVSSGTQ
ANLLALMSHC ERGDEYLCGQ QAHNYKFEGG GAAVLGSIQP QPLNNQADGS ILLSDIEAAI
KSDDVHFART RLLSLENTIG GKVLNQDYLA QAQSLAFNRG LKIHLDGARV ANAAVAQGIA
IADITQYFDS VSICLSKGLC APIGSILLGD ERLIGKATRW RKMLGGGMRQ AGIIAAAAKL
ALTEQVDRLA DDHHNAKTLA LLLAEMNELT VDVSLVQTNM VFATIAEHID PRVLTAKLAD
KGIIISPSRQ LRLVTHNNIS ANDISVFVNA LKQIIR
//
