ID U9W1K8_9CYAN Unreviewed; 408 AA.
AC U9W1K8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN ORFNames=N836_32565 {ECO:0000313|EMBL:ESA38167.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA38167.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA38167.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA38167.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESA38167.1}.
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DR EMBL; AWNH01000014; ESA38167.1; -; Genomic_DNA.
DR RefSeq; WP_023070938.1; NZ_AWNH01000014.1.
DR AlphaFoldDB; U9W1K8; -.
DR STRING; 1385935.N836_32565; -.
DR PATRIC; fig|1385935.3.peg.870; -.
DR eggNOG; COG1171; Bacteria.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000017515; Unassembled WGS sequence.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR CDD; cd04886; ACT_ThrD-II-like; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR044561; ACT_ThrD-II-like.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01127; ilvA_1Cterm; 1.
DR PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51671; ACT; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000017515}.
FT DOMAIN 326..405
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 408 AA; 43937 MW; 67CCEE2387474CF9 CRC64;
MTITLDQIRQ AAQQIHSGIV HTPCVYSTKL SQLTNTRVAL KFENLQFTGS FKDRGSLCKL
LSLSTTQQQQ GVVAMSAGNH GQAVAYHAQR LGIPAVIVMP QFTPSVKVER TQSFGAEIHL
YGDTLDAAKT LAQQLAQERQ LTLIHPYDDS FIIVGQGTVA IEMLKDCPDL DSIIVPIGGG
GLISGIAIAA KQMRPSINII GVQTTRYPSM YQAIAGKQLC FGCSTIAEGI AVKTPGSLTL
PIVQNLVDDI VLVEETEIEQ AVRLLLEVEK IVVEGAGAVG LAALLKEHER FTGKTVGIVL
SGGNIDLLIL SSILQRSLVR DQRLVRLQVN IRDIPGALAA VSQIIAETQA NIVGVEHHRM
FTGLPVQSAI LEFSLLIRGH QHLNQILNML KTAGHDAHSL PLDTEVPG
//
