ID   Q8TM10_METAC            Unreviewed;       503 AA.
AC   Q8TM10;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=Aldehyde dehydrogenase (NAD+) {ECO:0000313|EMBL:AAM06239.1};
GN   Name=aldH {ECO:0000313|EMBL:AAM06239.1};
GN   OrderedLocusNames=MA_2860 {ECO:0000313|EMBL:AAM06239.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM06239.1, ECO:0000313|Proteomes:UP000002487};
RN   [1] {ECO:0000313|EMBL:AAM06239.1, ECO:0000313|Proteomes:UP000002487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC   {ECO:0000313|Proteomes:UP000002487};
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA   Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA   Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA   de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA   Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA   Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AE010299; AAM06239.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TM10; -.
DR   STRING; 188937.MA_2860; -.
DR   EnsemblBacteria; AAM06239; AAM06239; MA_2860.
DR   KEGG; mac:MA_2860; -.
DR   HOGENOM; CLU_005391_0_0_2; -.
DR   InParanoid; Q8TM10; -.
DR   PhylomeDB; Q8TM10; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   CDD; cd07131; ALDH_AldH-CAJ73105; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002487}.
FT   DOMAIN          28..487
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   503 AA;  54757 MW;  5DB538F2B7411BCB CRC64;
     MVLYSLFQGD FVVQEYKLHI GGESRDSATG ETFDNINPAT LENLATVQVA GSEDVDRAVE
     AAEEGFRVWS EVPAPRRAEV LFRTARILQE RKEDLARLMT EEMGKVLPET RGDVQEAIDI
     AIYAAGEGRR MFGETTTSEL KDKFCMTVLR PIGVVGMITP WNFPLAIPGW KIMPALIAGN
     AIVFKPASDT PLLAIKLVEI LMEAGLPPGV VNLVTGPGGS TGKAIVQHPR IKAISFTGSL
     ETGKWIMEEC AKTMKRVSLE LGGKNPVIIM DDADLELALE GVLWGAFGTT GQRCTATSRL
     ILHEKIKDEF TARLLAKTKL LRVGNGLLPE TDIGPIINKA QLEKIERYVR IGMEEGATLL
     LGGKAIDPGL PGYFFEPTVF TDVRPDMRIA QEEIFGPVLS IITVSGLEEA IEVANNTRYG
     LSSAIYTENV GKAFRAVKKI EAGITYVNAP TIGAEVHLPF GGVKGTGNGF REAGTEAIKE
     FTEIKAVYID YSGRLQRAQI DME
//