ID   O52942_PHOLP            Unreviewed;       361 AA.
AC   O52942;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   SubName: Full=Alanine dehydrogenase;
DE            EC=1.4.1.1;
GN   Name=ald;
OS   Phormidium lapideum.
OC   Bacteria; Cyanobacteria; Oscillatoriales; Phormidium.
OX   NCBI_TaxID=32060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sawa Y., Noshiro Y., Midorikawa Y., Sasai R., Murata K., Ashida H.,
RA   Shibata H., Ochiai H.;
RT   "Alanine Dehydrogenase from a Cyanobacterium, Phormidium lapideum:
RT   Cloning, Sequencing, Expression, and Sequence Comparisons to Amino
RT   Acid Dehydrogenases.";
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=95204408; PubMed=7896761;
RA   Sawa Y., Tani M., Murata K., Shibata H., Ochiai H.;
RT   "Purification and characterization of alanine dehydrogenase from a
RT   cyanobacterium, Phormidium lapideum.";
RL   J. Biochem. 116:995-1000(1994).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=98100077; PubMed=9437424; DOI=10.1038/nsb0198-19;
RA   Schultz J., Hoffmuller U., Krause G., Ashurst J., Macias M.J.,
RA   Schmieder P., Schneider-Mergener J., Oschkinat H.;
RT   "Specific interactions between the syntrophin PDZ domain and voltage-
RT   gated sodium channels.";
RL   Nat. Struct. Biol. 5:19-24(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   MEDLINE=98328106; PubMed=9665169; DOI=10.1038/817;
RA   Baker P.J., Sawa Y., Shibata H., Sedelnikova S.E., Rice D.W.;
RT   "Analysis of the structure and substrate binding of Phormidium
RT   lapideum alanine dehydrogenase.";
RL   Nat. Struct. Biol. 5:561-567(1998).
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DR   EMBL; D37807; BAA24455.1; -; Genomic_DNA.
DR   PIR; PX0078; PX0078.
DR   PDB; 1PJB; X-ray; 2.10 A; A=1-361.
DR   PDB; 1PJC; X-ray; 2.00 A; A=1-361.
DR   PDB; 1SAY; X-ray; 2.10 A; A=1-361.
DR   PDBsum; 1PJB; -.
DR   PDBsum; 1PJC; -.
DR   PDBsum; 1SAY; -.
DR   BioCyc; MetaCyc:MON-12816; -.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007698; Ala_DH/PNT_C.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; Ala_DH/PNT_N.
DR   InterPro; IPR008141; Ala_DH_PNT.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   TIGRFAMs; TIGR00518; alaDH; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase.
SQ   SEQUENCE   361 AA;  38557 MW;  57CA14BB85DB4D08 CRC64;
     MEIGVPKEIK NQEFRVGLSP SSVRTLVEAG HTVFIETQAG IGAGFADQDY VQAGAQVVPS
     AKDAWSREMV VKVKEPLPAE YDLMQKDQLL FTYLHLAAAR ELTEQLMRVG LTAIAYETVE
     LPNRSLPLLT PMSIIAGRLS VQFGARFLER QQGGRGVLLG GVPGVKPGKV VILGGGVVGT
     EAAKMAVGLG AQVQIFDINV ERLSYLETLF GSRVELLYSN SAEIETAVAE ADLLIGAVLV
     PGRRAPILVP ASLVEQMRTG SVIVDVAVDQ GGCVETLHPT SHTQPTYEVF GVVHYGVPNM
     PGAVPWTATQ ALNNSTLPYV VKLANQGLKA LETDDALAKG LNVQAHRLVH PAVQQVFPDL
     A
//