ID   A0A241V4C3_9GAMM        Unreviewed;       713 AA.
AC   A0A241V4C3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Haloacid dehalogenase {ECO:0000313|EMBL:OTG68032.1};
GN   ORFNames=B9T38_16265 {ECO:0000313|EMBL:OTG68032.1};
OS   Acinetobacter sp. ANC 4218.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977880 {ECO:0000313|EMBL:OTG68032.1, ECO:0000313|Proteomes:UP000194947};
RN   [1] {ECO:0000313|EMBL:OTG68032.1, ECO:0000313|Proteomes:UP000194947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4218 {ECO:0000313|EMBL:OTG68032.1,
RC   ECO:0000313|Proteomes:UP000194947};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OTG68032.1}.
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DR   EMBL; NEGD01000026; OTG68032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241V4C3; -.
DR   STRING; 1977880.B9T38_16265; -.
DR   OrthoDB; 9800058at2; -.
DR   Proteomes; UP000194947; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd07505; HAD_BPGM-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   PANTHER; PTHR46193; 6-PHOSPHOGLUCONATE PHOSPHATASE; 1.
DR   PANTHER; PTHR46193:SF22; HEXITOL PHOSPHATASE B; 1.
DR   Pfam; PF13419; HAD_2; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          509..655
FT                   /note="Mannitol dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08125"
SQ   SEQUENCE   713 AA;  80852 MW;  6519794F67A73AB4 CRC64;
     MLKFNNDIIH GAIFDMDGTM FDTERLRFQT LKQASQELIG VSFSDAYLMA CLGLSASSAH
     QLAKQQYGDD IPYAEIRQRA DELELESVRS LGVPIKKGLV QVLERLRKSG LRMAVATSSR
     RLIAEEYLIN ANVYKFFDVL VCGDEVQKGK PHPEIFLSAA EKLNLPTSEC LMFEDSENGI
     TSAYNAGGVT ILLQDIKEPN SNMLAKTDYF FESMYDCLHQ LDQHTLNLEM PTLQESFPQS
     LNQLTVGIHG FGAIGGGFMA QILSHWDGYT RPKRIYASTH NSLYRSAVNA FGSYCIRYGQ
     LSYDERIENM HIIDAGNIEQ MQEMYIASSM IAVCLPEQAI ATEARTIAQG LYARHIANNE
     QFTNPLTVLI ILNKIGAKHL LLEHVHSALV EITAPDIAEQ ILEQHYFCDT VVNRMVSKLT
     DQNLYRQLRI KYNIFKQYQL DHDLDHADIE DATRLNPEQE RLASMYVEEM CSNFKPSHIL
     QTMDLILFHA EVDMPIYVEN NSPLLGKMRQ MVLVDDIQEI QLIKNRLWNG VHAMTTWYAT
     RLGYETIGLA MADPKVREFM EGLLEEVKAG LTLTLPHRKN DLDDLAKSFI NSCVNAYKDP
     CERVARDPLR KLAASERVLG SIACNIQQGL PYQNLSQGAL YGYYYSIQQK DISYGEAIEH
     LKIQLGQSGL NEQHQQTLQR NIETQLAQLL PAKHKTHNPH CVDLAKQMDH SLT
//