DIALD_STAA8
ID DIALD_STAA8 Reviewed; 459 AA.
AC Q2FWX9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=4,4'-diaponeurosporen-aldehyde dehydrogenase {ECO:0000303|PubMed:22535955};
DE EC=1.2.1.- {ECO:0000269|PubMed:22535955};
DE AltName: Full=4,4'-diaponeurosporenal dehydrogenase {ECO:0000305|PubMed:22535955};
GN Name=aldH1 {ECO:0000303|PubMed:22535955};
GN OrderedLocusNames=SAOUHSC_02142 {ECO:0000312|EMBL:ABD31190.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000312|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=KCTC 1928, and RN4220;
RX PubMed=22535955; DOI=10.1074/jbc.m112.343020;
RA Kim S.H., Lee P.C.;
RT "Functional expression and extension of staphylococcal staphyloxanthin
RT biosynthetic pathway in Escherichia coli.";
RL J. Biol. Chem. 287:21575-21583(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the yellow-orange carotenoid
CC staphyloxanthin, which plays a role in the virulence via its protective
CC function against oxidative stress. Catalyzes the oxidation of 4,4'-
CC diaponeurosporen-4-al to yield 4,4'-diaponeurosporenoic acid.
CC {ECO:0000269|PubMed:22535955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4'-diaponeurosporenal + H2O + NAD(+) = 4,4'-
CC diaponeurosporenoate + 2 H(+) + NADH; Xref=Rhea:RHEA:42384,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:79064, ChEBI:CHEBI:79065;
CC Evidence={ECO:0000269|PubMed:22535955};
CC -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC staphyloxanthin from farnesyl diphosphate.
CC {ECO:0000269|PubMed:22535955}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC staphyloxanthin and cause accumulation of 4,4'- diaponeurosporen-4-al.
CC {ECO:0000269|PubMed:22535955}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31190.1; -; Genomic_DNA.
DR RefSeq; WP_001021214.1; NZ_LS483365.1.
DR RefSeq; YP_500632.1; NC_007795.1.
DR PDB; 6K0Z; X-ray; 2.50 A; A=1-459.
DR PDB; 6K10; X-ray; 1.79 A; A=1-459.
DR PDBsum; 6K0Z; -.
DR PDBsum; 6K10; -.
DR AlphaFoldDB; Q2FWX9; -.
DR SMR; Q2FWX9; -.
DR STRING; 1280.SAXN108_2023; -.
DR EnsemblBacteria; ABD31190; ABD31190; SAOUHSC_02142.
DR GeneID; 3921839; -.
DR KEGG; sao:SAOUHSC_02142; -.
DR PATRIC; fig|93061.5.peg.1943; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_3_1_9; -.
DR OMA; RHGKRWM; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carotenoid biosynthesis; NAD; Oxidoreductase;
KW Reference proteome; Virulence.
FT CHAIN 1..459
FT /note="4,4'-diaponeurosporen-aldehyde dehydrogenase"
FT /id="PRO_0000444879"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 114..115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 188..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 64..82
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:6K10"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 257..272
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:6K10"
FT HELIX 418..423
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:6K10"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:6K0Z"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:6K0Z"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:6K10"
SQ SEQUENCE 459 AA; 51741 MW; 878E3BE00ABCDA55 CRC64;
MNIIEQKFYD SKAFFNTQQT KDISFRKEQL KKLSKAIKSY ESDILEALYT DLGKNKVEAY
ATEIGITLKS IKIARKELKN WTKTKNVDTP LYLFPTKSYI KKEPYGTVLI IAPFNYPFQL
VFEPLIGAIA AGNTAIIKPS ELTPNVARVI KRLINETFDA NYIEVIEGGI EETQTLIHLP
FDYVFFTGSE NVGKIVYQAA SENLVPVTLE MGGKSPVIVD ETANIKVASE RICFGKFTNA
GQTCVAPDYI LVHESVKDDL ITALSKTLRE FYGQNIQQSP DYGRIVNLKH YHRLTSLLNS
AQMNIVFGGH SDEDERYIEP TLLDHVTSDS AIMQEEIFGP ILPILTYQSL DEAIAFIHQR
PKPLSLYLFS EDENATQRVI NELSFGGGAI NDTLMHLANP KLPFGGVGAS GMGRYHGKYS
FDTFTHEKSY IFKSTRLESG VHLPPYKGKF KYIKAFFKN
