ID HPBD_SALBH Reviewed; 367 AA. AC Q0FPQ4; DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 24-JAN-2024, entry version 77. DE RecName: Full=4-hydroxyproline betaine 2-epimerase; DE Short=Hyp-B 2-epimerase; DE EC=5.1.1.22 {ECO:0000269|PubMed:24056934}; DE AltName: Full=(4R)-4-hydroxyproline betaine 2-epimerase; GN Name=hpbD; ORFNames=R2601_01638; OS Salipiger bermudensis (strain DSM 26914 / JCM 13377 / KCTC 12554 / OS HTCC2601) (Pelagibaca bermudensis). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Salipiger. OX NCBI_TaxID=314265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 26914 / JCM 13377 / KCTC 12554 / HTCC2601; RX PubMed=20729358; DOI=10.1128/jb.00873-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter RT genera."; RL J. Bacteriol. 192:5552-5553(2010). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM AND RP HYDROXYPROLINE BETAINE, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, RP COFACTOR, GENE NAME, AND PATHWAY. RC STRAIN=DSM 26914 / JCM 13377 / KCTC 12554 / HTCC2601; RX PubMed=24056934; DOI=10.1038/nature12576; RA Zhao S., Kumar R., Sakai A., Vetting M.W., Wood B.M., Brown S., RA Bonanno J.B., Hillerich B.S., Seidel R.D., Babbitt P.C., Almo S.C., RA Sweedler J.V., Gerlt J.A., Cronan J.E., Jacobson M.P.; RT "Discovery of new enzymes and metabolic pathways by using structure and RT genome context."; RL Nature 502:698-702(2013). CC -!- FUNCTION: Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline CC betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is CC involved in a catabolic pathway that degrades tHyp-B to alpha- CC ketoglutarate. This pathway would permit the utilization of tHyp-B as a CC carbon and nitrogen source in the absence of osmotic stress, since CC tHyp-B functions as an osmolyte and is not catabolized when it is CC needed as osmoprotectant. To a lesser extent, can also catalyze the CC racemization of L-proline betaine. {ECO:0000269|PubMed:24056934}. CC -!- CATALYTIC ACTIVITY: CC Reaction=trans-4-hydroxy-L-proline betaine = cis-4-hydroxy-D-proline CC betaine; Xref=Rhea:RHEA:47544, ChEBI:CHEBI:85533, ChEBI:CHEBI:85534; CC EC=5.1.1.22; Evidence={ECO:0000269|PubMed:24056934}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-proline betaine = D-proline betaine; Xref=Rhea:RHEA:51884, CC ChEBI:CHEBI:35280, ChEBI:CHEBI:134398; EC=5.1.1.22; CC Evidence={ECO:0000269|PubMed:24056934}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:24056934}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24056934}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=42 mM for trans-4-hydroxy-L-proline betaine CC {ECO:0000269|PubMed:24056934}; CC KM=8 mM for L-proline betaine {ECO:0000269|PubMed:24056934}; CC Note=kcat is 330 sec(-1) with trans-4-hydroxy-L-proline betaine as CC substrate and 5.3 sec(-1) with L-proline betaine as substrate.; CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing CC enzyme family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AATQ01000017; EAU46159.1; -; Genomic_DNA. DR RefSeq; WP_007801489.1; NZ_DS022277.1. DR PDB; 2PMQ; X-ray; 1.72 A; A/B=2-367. DR PDB; 4H2H; X-ray; 1.70 A; A/B/C/D/E/F/G/H=2-367. DR PDBsum; 2PMQ; -. DR PDBsum; 4H2H; -. DR AlphaFoldDB; Q0FPQ4; -. DR SMR; Q0FPQ4; -. DR DIP; DIP-60607N; -. DR STRING; 314265.R2601_01638; -. DR eggNOG; COG4948; Bacteria. DR HOGENOM; CLU_030273_4_5_5; -. DR OrthoDB; 9802699at2; -. DR BioCyc; MetaCyc:MONOMER-18940; -. DR BRENDA; 5.1.1.22; 15071. DR EvolutionaryTrace; Q0FPQ4; -. DR Proteomes; UP000006230; Unassembled WGS sequence. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0036361; F:racemase activity, acting on amino acids and derivatives; IDA:UniProtKB. DR GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IDA:CACAO. DR GO; GO:0006579; P:amino-acid betaine catabolic process; ISS:UniProtKB. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1. DR InterPro; IPR034622; 4R-hPro_betaine_2-epimerase. DR InterPro; IPR034593; DgoD-like. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR029017; Enolase-like_N. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR013342; Mandelate_racemase_C. DR InterPro; IPR013341; Mandelate_racemase_N_dom. DR PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1. DR PANTHER; PTHR48080:SF3; ENOLASE SUPERFAMILY MEMBER DDB_G0284701; 1. DR Pfam; PF13378; MR_MLE_C; 1. DR Pfam; PF02746; MR_MLE_N; 1. DR SFLD; SFLDF00556; 4R-hydroxyproline_betaine_2-ep; 1. DR SFLD; SFLDG00180; muconate_cycloisomerase; 1. DR SMART; SM00922; MR_MLE; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Isomerase; Magnesium; Metal-binding; Reference proteome. FT CHAIN 1..367 FT /note="4-hydroxyproline betaine 2-epimerase" FT /id="PRO_0000425278" FT ACT_SITE 163 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 265 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="substrate" FT BINDING 161 FT /ligand="substrate" FT BINDING 193 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 218 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 241 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 294 FT /ligand="substrate" FT STRAND 2..15 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 27..39 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 61..73 FT /evidence="ECO:0007829|PDB:4H2H" FT TURN 74..77 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 82..92 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 97..115 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 119..122 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 142..155 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 169..183 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 200..209 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 224..230 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 247..255 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 272..285 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 298..308 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 313..315 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:4H2H" FT HELIX 323..325 FT /evidence="ECO:0007829|PDB:4H2H" FT TURN 332..334 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:4H2H" FT TURN 357..360 FT /evidence="ECO:0007829|PDB:4H2H" FT STRAND 364..367 FT /evidence="ECO:0007829|PDB:4H2H" SQ SEQUENCE 367 AA; 39558 MW; 6377860F2A17B87E CRC64; MKIAEIQLFQ HDLPVVNGPY RIASGDVWSL TTTIVKIIAE DGTIGWGETC PVGPTYAEAH AGGALAALEV LASGLAGAEA LPLPLHTRMD SLLCGHNYAK SALDIAVHDL WGKRLGVPVH ELLGGALTDS VSSYYSLGVM EPDEAARQAL EKQREGYSRL QVKLGARPIE IDIEAIRKVW EAVRGTGIAL AADGNRGWTT RDALRFSREC PDIPFVMEQP CNSFEDLEAI RPLCHHALYM DEDGTSLNTV ITAAATSLVD GFGMKVSRIG GLQHMRAFRD FCAARNLPHT CDDAWGGDIV SAACTHIAST VLPRLMEGAW LAQPYVAEHY DAENGVRIEG GRIRVPQGPG LGLTIDPERF GPPLFSA //