ID   DHMA_FLAS1              Reviewed;         271 AA.
AC   P22441;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=N-acylmannosamine 1-dehydrogenase;
DE            Short=NAM-DH;
DE            EC=1.1.1.233;
OS   Flavobacterium sp. (strain 141-8).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium; unclassified Flavobacterium.
OX   NCBI_TaxID=240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1854199; DOI=10.1128/aem.57.5.1418-1422.1991;
RA   Yamamoto-Otake H., Koyama Y., Horiuchi T., Nakano E.;
RT   "Cloning, sequencing, and expression of the N-acyl-D-mannosamine
RT   dehydrogenase gene from Flavobacterium sp. strain 141-8 in Escherichia
RT   coli.";
RL   Appl. Environ. Microbiol. 57:1418-1422(1991).
CC   -!- FUNCTION: Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-D-mannosamine + NAD(+) = an N-acyl-D-
CC         mannosaminolactone + H(+) + NADH; Xref=Rhea:RHEA:11540,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16062, ChEBI:CHEBI:17970,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.233;
CC   -!- MISCELLANEOUS: NAM-DH may be applicable to the quantitative
CC       determination of sialic acid in serum.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; D90316; BAA14346.1; -; Genomic_DNA.
DR   PIR; A43744; A43744.
DR   PDB; 4CR6; X-ray; 1.90 A; A/B/C/D=1-271.
DR   PDB; 4CR7; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-271.
DR   PDB; 4CR8; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-271.
DR   PDBsum; 4CR6; -.
DR   PDBsum; 4CR7; -.
DR   PDBsum; 4CR8; -.
DR   AlphaFoldDB; P22441; -.
DR   SMR; P22441; -.
DR   BRENDA; 1.1.1.233; 2302.
DR   GO; GO:0050123; F:N-acylmannosamine 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..271
FT                   /note="N-acylmannosamine 1-dehydrogenase"
FT                   /id="PRO_0000054635"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         20..44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   TURN            12..15
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          17..22
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           26..37
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           48..52
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           72..85
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          90..93
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           109..119
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           121..136
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   TURN            137..142
FT                   /evidence="ECO:0007829|PDB:4CR7"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           164..184
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          189..196
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           211..220
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           229..240
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          251..255
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           258..260
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   HELIX           264..266
FT                   /evidence="ECO:0007829|PDB:4CR6"
FT   TURN            268..270
FT                   /evidence="ECO:0007829|PDB:4CR6"
SQ   SEQUENCE   271 AA;  27469 MW;  7346D6E7EF459762 CRC64;
     MTTAGVSRRP GRLAGKAAIV TGAAGGIGRA TVEAYLREGA SVVAMDLAPR LAATRYEEPG
     AIPIACDLAD RAAIDAAMAD AVARLGGLDI LVAGGALKGG TGNFLDLSDA DWDRYVDVNM
     TGTFLTCRAG ARAMVAAGAG KDGRSARIIT IGSVNSFMAE PEAAAYVAAK GGVAMLTRAM
     AVDLARHGIL VNMIAPGPVD VTGNNTGYSE PRLAEQVLDE VALGRPGLPE EVATAAVFLA
     EDGSSFITGS TITIDGGLSA MIFGGMREGR R