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Database: UniProt
Entry: R5CSV4_9BACT
LinkDB: R5CSV4_9BACT
Original site: R5CSV4_9BACT 
ID   R5CSV4_9BACT            Unreviewed;       368 AA.
AC   R5CSV4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   18-JUL-2018, entry version 20.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|PIRNR:PIRNR000183};
GN   ORFNames=BN458_00300 {ECO:0000313|EMBL:CCX66796.1};
OS   Prevotella sp. CAG:1058.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella; environmental samples.
OX   NCBI_TaxID=1262918 {ECO:0000313|EMBL:CCX66796.1, ECO:0000313|Proteomes:UP000018314};
RN   [1] {ECO:0000313|EMBL:CCX66796.1, ECO:0000313|Proteomes:UP000018314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1058 {ECO:0000313|Proteomes:UP000018314};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3)
CC       + NADH. {ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step
CC       1/1. {ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCX66796.1}.
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DR   EMBL; CAWU010000164; CCX66796.1; -; Genomic_DNA.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000018314; Unassembled WGS sequence.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05305; L-AlaDH; 1.
DR   InterPro; IPR008141; Ala_DH.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR008142; AlaDH/PNT_CS1.
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; PTHR42795; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF000183; Alanine_dh; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00518; alaDH; 1.
DR   PROSITE; PS00836; ALADH_PNT_1; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018314};
KW   NAD {ECO:0000256|PIRNR:PIRNR000183, ECO:0000256|PIRSR:PIRSR000183-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018314}.
FT   DOMAIN        4    137       AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}.
FT   DOMAIN      149    297       AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}.
FT   NP_BIND     239    240       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   NP_BIND     267    270       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   ACT_SITE     96     96       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   ACT_SITE    270    270       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   BINDING      15     15       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING      75     75       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING     134    134       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     198    198       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     220    220       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
SQ   SEQUENCE   368 AA;  39199 MW;  85AEFD7CFB7F07F9 CRC64;
     MKIGIPKEIK NNENRVGMTP AGVSELIKHG HSVYVQKTAG EGSGFTDDMY LSVGAQILPS
     IEDVYATADM IIKVKEPISP EYPLIRKGQL VFTYFHFACS RELTEAMVKS GGVCLAYETV
     QLADGSLPLL VPMSEIAGRM ATINGTYYLQ KTKGGKGKLI CGVPGVMPTK VVVIGGGIVG
     QAAARMAAGM GADVVIADIS LPLLHELSIN MPANVNTLYS SAQNIGKEIK DADIIIGAVL
     VPGDKAPKLI TREMLKTMEP GTILVDVAID QGGCFETSHP TTHSEPTYEV DGIVHYAVAN
     IPGAVPNTST TALTNATLKY AIALADKGWR EACRENQALY KGLNIVEGKI TYKAVADVFN
     MPYEPISL
//
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