ID U2YAS6_STRCV Unreviewed; 883 AA.
AC U2YAS6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=ANG5_0380 {ECO:0000313|EMBL:GAD43852.1};
OS Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1035184 {ECO:0000313|EMBL:GAD43852.1, ECO:0000313|Proteomes:UP000016985};
RN [1] {ECO:0000313|EMBL:GAD43852.1, ECO:0000313|Proteomes:UP000016985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG46377 {ECO:0000313|Proteomes:UP000016985};
RA Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y.,
RA Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., Hayashi T.,
RA Shintani S.;
RT "Genome Sequences of seven clinical isolates and type strains of anginosus
RT group streptococci.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000256|ARBA:ARBA00035645,
CC ECO:0000256|PIRNR:PIRNR000111}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00035641,
CC ECO:0000256|PIRNR:PIRNR000111}.
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:GAD43852.1}.
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DR EMBL; BASX01000002; GAD43852.1; -; Genomic_DNA.
DR RefSeq; WP_020997530.1; NZ_BASX01000002.1.
DR AlphaFoldDB; U2YAS6; -.
DR Proteomes; UP000016985; Unassembled WGS sequence.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd08178; AAD_C; 1.
DR CDD; cd07122; ALDH_F20_ACDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald-ADH.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000111}.
FT DOMAIN 14..419
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 473..863
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 883 AA; 96614 MW; 3F67D8356254178A CRC64;
MADKKTLTPE EKKLAAEKHV DELVQKGLIA LEEMRKLNQE QVDYIVAKAS VAALDAHGIL
AEHAVKETGR GVFEDKATKN LFACEHVVNN MRGVKTVGVI EDDPITGLTK IAEPVGVICG
VTPTTNPTST AIFKSLISLK TRNPIVFAFH PSAQESSVHA AQIVCDAAIA AGAPENCVQW
ITQPSMEATT ALMNHEGIAT ILATGGNAMV KAAYSCGKPA LGVGAGNVPA YVEKSANIRQ
AAHDIVMSKS FDNGMVCASE QAVIIDKEIY DEFVEEFKSY HTYFVNKKEK ALLEEFCFGA
KANSKNCAGA KLNPNIVGKS AVWIAEQAGF KVPEGTNILA AECAEVGPNE PLTREKLSPV
IAVLKAEDTE DGLTKARQMV EFNGLGHSAA IHTKDEALAK RFGTEIKAMR IIWNSPSTFG
GIGDVYNAFI PSLTLGCGSY GRNSVGDNVS AINLLNIKKV GKRRNNMQWF KVPSKIYFER
NSIQYLQTCE DIERVMIVTD KSIEKLGFVQ RVIDQLNLRK NKVTIQVFSD VEPDPDITTI
RRGTEEMRAF EPDTIIALGG GSPMDAAKGM WMFYEQPEVD FSDLVQKFMD IRKRAFKFPS
LGKKAKYIGI PTTSGTGSEV TPFAVISDKA NNCKYPLADY ALTPTIAIVD PALVESVPAF
IAADTGMDVL THATEAYTSN FANDYTDGIA LQTIKLVFKY LEKSVKTADP EAREKMHNAS
TMAGMAFANA FLGMSHSMAH KIGGVHHTIH GRTNAILLPY VIRYNGTRPS KTTTWPKYNY
WKADEKFQDI ARMLGLPCST PEEAVEAYAK AVYDLGVAVG IKMNFKDQGI DEKVWNESLH
EIALLAYEDQ CSPANPRLPM VADMEEIMAD AYYGYAERPG RRK
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