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Database: UniProt
Entry: M7NFP8_9BACT
LinkDB: M7NFP8_9BACT
Original site: M7NFP8_9BACT 
ID   M7NFP8_9BACT            Unreviewed;       385 AA.
AC   M7NFP8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE            EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN   Name=ald2 {ECO:0000313|EMBL:EMR00650.1};
GN   ORFNames=ADICEAN_04228 {ECO:0000313|EMBL:EMR00650.1};
OS   Cesiribacter andamanensis AMV16.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC   Cesiribacter.
OX   NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR00650.1, ECO:0000313|Proteomes:UP000011910};
RN   [1] {ECO:0000313|EMBL:EMR00650.1, ECO:0000313|Proteomes:UP000011910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMV16 {ECO:0000313|EMBL:EMR00650.1,
RC   ECO:0000313|Proteomes:UP000011910};
RX   PubMed=23682146;
RA   Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT   from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL   Genome Announc. 1:E00240-13(2013).
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005689}.
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:EMR00650.1}.
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DR   EMBL; AODQ01000219; EMR00650.1; -; Genomic_DNA.
DR   RefSeq; WP_009197602.1; NZ_AODQ01000219.1.
DR   AlphaFoldDB; M7NFP8; -.
DR   STRING; 1279009.ADICEAN_04228; -.
DR   PATRIC; fig|1279009.4.peg.4250; -.
DR   eggNOG; COG0686; Bacteria.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000011910; Unassembled WGS sequence.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR   CDD; cd05305; L-AlaDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008141; Ala_DH.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EMR00650.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011910}.
FT   DOMAIN          14..147
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          159..307
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   385 AA;  41853 MW;  FD40CF5455F26232 CRC64;
     MLELKQGNKH LLIGIPKERA MQENRVALTP EAVALLVNNG HEVWVEKGAG DTAKYTDQEY
     SNAGAQIKYT SKEVFEAEIV LKVEPPTDEE IGYIRPGKTL ISALQVGNQK EEFIHKLNKK
     RITAIAFELL EDKVGGMPVV RAMSEIAGSA VMLIAAEYLS STASGKGIIL GGITGVPPTK
     VVILGAGTVG EYAARTALGL GAEVQVYDTH LYKLRRIRQS LGHHLYTSTL DPATVANSLK
     TADVVVGAIR AEKGRSKIVV TDQMVMSMKP GSIIIDVGID QGGCVETSEI TTHSKPVFLK
     HEIIHYCVPN IPSRVARTAT QAFSNIFSPI LLQAADVGGI DEMIFTNKWF MNGVYTYKGF
     LSNQHVARKF GLKHKDLSLL MAARN
//
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