TNAA_HALSA
ID TNAA_HALSA Reviewed; 448 AA.
AC Q9HMV2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Probable tryptophanase;
DE EC=4.1.99.1;
DE AltName: Full=L-tryptophan indole-lyase;
DE Short=TNase;
GN Name=tnaA; OrderedLocusNames=VNG_2373G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tryptophan = indole + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:19553, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16881, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; EC=4.1.99.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG20469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG20469.1; ALT_INIT; Genomic_DNA.
DR PIR; A84388; A84388.
DR RefSeq; WP_012289493.1; NC_002607.1.
DR AlphaFoldDB; Q9HMV2; -.
DR SMR; Q9HMV2; -.
DR STRING; 64091.VNG_2373G; -.
DR PaxDb; Q9HMV2; -.
DR EnsemblBacteria; AAG20469; AAG20469; VNG_2373G.
DR GeneID; 5953359; -.
DR KEGG; hal:VNG_2373G; -.
DR PATRIC; fig|64091.14.peg.1837; -.
DR HOGENOM; CLU_047223_0_0_2; -.
DR InParanoid; Q9HMV2; -.
DR OrthoDB; 24775at2157; -.
DR PhylomeDB; Q9HMV2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00544; Tryptophanase; 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR011166; Beta-eliminating_lyase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR013440; TNase.
DR InterPro; IPR018176; Tryptophanase_CS.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF001386; Trpase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..448
FT /note="Probable tryptophanase"
FT /id="PRO_0000195630"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 448 AA; 48121 MW; B1AF82C45494C139 CRC64;
MRSHTATMVD RIEDTSRADR EAALADAGHN VFELASDDVA VDLLTDSGTG TMSNDQWAAM
LQGDEAYAGS ASFEDLAVAA EDVMGFQHII PAHQGRGAEN VLYGAVLSAG DTVLNNAHFD
TTRAHVAAND ATPVDCPVDG ARDPDTDAPF KGNFSVERAR RVVDDVGADA VPVVVLTITN
NSMAGQPVSI ENTREVAAFA DDIDATFVID ACRFAENAHF VQQREPGYEH DSVAAIAREQ
LSYADACVMS GKKDGLVNVG GFVGLHDDGR LHEQCRQRGI LYEGFSTYGG MSGRDMAAFA
VGLREAVEPP YVAERVAQVQ RLADALTDRD VPIYQPAGGH AVYIDANAAL PHLPREQFPG
QAFVCELYRE GGVRAVELGR FAFPDTDRRD LVRLALPRRT YGPDHLDHVA DTAAAVCERG
TDVTGLEIVS EPELTELRHF SAALQPVA