ID B9LND5_HALLT Unreviewed; 348 AA.
AC B9LND5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase {ECO:0000313|EMBL:ACM56873.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:ACM56873.1};
GN OrderedLocusNames=Hlac_1281 {ECO:0000313|EMBL:ACM56873.1};
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM56873.1, ECO:0000313|Proteomes:UP000000740};
RN [1] {ECO:0000313|EMBL:ACM56873.1, ECO:0000313|Proteomes:UP000000740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC {ECO:0000313|Proteomes:UP000000740};
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001365; ACM56873.1; -; Genomic_DNA.
DR RefSeq; WP_015910015.1; NC_012029.1.
DR AlphaFoldDB; B9LND5; -.
DR GeneID; 7399376; -.
DR KEGG; hla:Hlac_1281; -.
DR eggNOG; arCOG00118; Archaea.
DR HOGENOM; CLU_029381_0_4_2; -.
DR Proteomes; UP000000740; Chromosome 1.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06502; TA_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; 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:ACM56873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000740}.
FT DOMAIN 9..292
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 348 AA; 36795 MW; 1DE0C515526D222A CRC64;
MEIDEDTIDL RSDTVTTPSE AMREAARDAE VGDDVYRDDP TVNELERRAA DAVGTEAALY
VPSGTMANQI AVHVHTEPGQ ELLLERESHI YRWELAGASK LSGTQTRTID AGDRCVPTPE
SVREGLVEED LHRPGTGLLS LENTHNYRGG TAIPVNQITA AAEVARDADV PVHLDGARVF
NAAVALGVDA SEIVAPVDTV TFCLSKGLGA PVGSIVAGDE AFVEDARRVR KLFGGGMRQA
GMIAAPGLLA LENVDRLVDD HANAERLATG LDALDGIHAP EPDTNIVVAH TEDAGITASD
LVTACKDAGV GCVEFAEYTT RFTTHLDVDG DDIDAAIDRI GDVIAELA
//
